Expression vectors encoding epitopes of target-associated antigens and methods for their design

ABSTRACT

The invention disclosed herein is directed to methods of identifying a polypeptide suitable for epitope liberation including, for example, the steps of identifying an epitope of interest; providing a substrate polypeptide sequence including the epitope, wherein the substrate polypeptide permits processing by a proteasome; contacting the substrate polypeptide with a composition including the proteasome, under conditions that support processing of the substrate polypeptide by the proteasome; and assaying for liberation of the epitope. The invention further relates to vectors including a housekeeping epitope expression cassette and also vectors including epitope cluster regions. The housekeeping epitope(s) can be derived from a target-associated antigen. The housekeeping epitope can be liberatable, that is capable of liberation, from a translation product of the cassette by immunoproteasome processing. The invention also relates to a method of activating a T cell comprising contacting a substrate polypeptide with an APC and contacting the APC with a T cell.

CROSS REFERENCE TO RELATED APPLICATIONS

[0001] This application is a continuation of U.S. application Ser. No.10/292,413, filed on Nov. 7, 2002, entitled “EXPRESSION VECTORS ENCODINGEPITOPES OF TARGET-ASSOCIATED ANTIGENS AND METHODS FOR THEIR DESIGN,which claims priority under 35 U.S.C. § 119(e) to U.S. ProvisionalApplication No. 60/336,968, filed on Nov. 7, 2001, having the sametitle; both of which are hereby incorporated by reference in theirentirety.

BACKGROUND OF THE INVENTION

[0002] 1. Field of the Invention

[0003] The invention disclosed herein is directed to methods for thedesign of epitope-encoding vectors, and epitope cluster regions, for usein compositions, including for example, pharmaceutical compositionscapable of inducing an immune response in a subject to whom thecompositions are administered. The invention is further directed to thevectors themselves. The epitope(s) expressed using such vectors canstimulate a cellular immune response against a target cell displayingthe epitope(s).

[0004] 2. Description of the Related Art

[0005] The immune system can be categorized into two discrete effectorarms. The first is innate immunity, which involves numerous cellularcomponents and soluble factors that respond to all infectiouschallenges. The other is the adaptive immune response, which iscustomized to respond specifically to precise epitopes from infectiousagents. The adaptive immune response is further broken down into twoeffector arms known as the humoral and cellular immune systems. Thehumoral arm is centered on the production of antibodies by B-lymphocyteswhile the cellular arm involves the killer cell activity of cytotoxic TLymphocytes.

[0006] Cytotoxic T Lymphocytes (CTL) do not recognize epitopes on theinfectious agents themselves. Rather, CTL detect fragments of antigensderived from infectious agents that are displayed on the surface ofinfected cells. As a result antigens are visible to CTL only after theyhave been processed by the infected cell and thus displayed on thesurface of the cell.

[0007] The antigen processing and display system on the surface of cellshas been well established. CTL recognize short peptide antigens, whichare displayed on the surface in non-covalent association with class Imajor histocompatibility complex molecules (MHC). These class I peptidesare in turn derived from the degradation of cytosolic proteins.

SUMMARY OF THE INVENTION

[0008] The invention disclosed herein relates to the identification ofepitope cluster regions that are used to generate pharmaceuticalcompositions capable of inducing an immune response from a subject towhom the compositions have been administered. One embodiment of thedisclosed invention relates to an epitope cluster, the cluster beingderived from an antigen associated with a target, the cluster includingor encoding at least two sequences having a known or predicted affinityfor an MHC receptor peptide binding cleft, wherein the cluster is anincomplete fragment of the antigen.

[0009] In one aspect of the invention, the target is a neoplastic cell.

[0010] In another aspect of the invention, the MHC receptor may be aclass I HLA receptor.

[0011] In yet another aspect of the invention, the cluster includes orencodes a polypeptide having a length, wherein the length is at least 10amino acids. Advantageously, the length of the polypeptide may be lessthan about 75 amino acids.

[0012] In still another aspect of the invention, there is provided anantigen having a length, wherein the cluster consists of or encodes apolypeptide having a length, wherein the length of the polypeptide isless than about 80% of the length of the antigen. Preferably, the lengthof the polypeptide is less than about 50% of the length of the antigen.Most preferably, the length of the polypeptide is less than about 20% ofthe length of the antigen.

[0013] Embodiments of the invention particularly relate to epitopeclusters identified in the tumor-associated antigen SSX-2 (SEQ ID NO:40). One embodiment of the invention relates to an isolated nucleic acidcontaining a reading frame with a first sequence encoding one or moresegments of SSX-2, wherein the whole antigen is not encoded, whereineach segment contains an epitope cluster, and wherein each clustercontains at least two amino acid sequences with a known or predictedaffinity for a same MHC receptor peptide binding cleft. In variousaspects of the invention the epitope cluster can be amino acids 5-28,16-28, 41-65, 57-67, 99-114, 167-180, and 167-183 of SSX-2. In otheraspects the segments can consist of an epitope cluster; the firstsequence can be a fragment of SSX-2; the fragment can consists of apolypeptide having a length, wherein the length of the polypeptide isless than about 90, 80, 60, 50, 25, or 10% of the length of SSX-2; thefragment can consist essentially of an amino acid sequence beginning atamino acid 5, 16, 41, 57, or 99 and ending at amino acid 65, 67, 114,180, or 183 of SSX-2; or the fragment consists of amino acids 15-183 ofSSX-2. Further embodiments of the invention include a second sequenceencoding essentially a housekeeping epitope. In one aspect of thisembodiment the first and second sequences constitute a single readingframe. In aspects of the invention the reading frame is operably linkedto a promoter. Other embodiments of the invention include thepolypeptides encoded by the nucleic acid embodiments of the inventionand immunogenic compositions containing the nucleic acids orpolypeptides of the invention.

[0014] Embodiments of the invention provide expression cassettes, forexample, for use in vaccine vectors, which encode one or more embeddedhousekeeping epitopes, and methods for designing and testing suchexpression cassettes. Housekeeping epitopes can be liberated from thetranslation product of such cassettes through proteolytic processing bythe immunoproteasome of professional antigen presenting cells (pAPC). Inone embodiment of the invention, sequences flanking the housekeepingepitope(s) can be altered to promote cleavage by the immunoproteasome atthe desired location(s). Housekeeping epitopes, their uses, andidentification are described in U.S. patent application Ser. Nos.09/560,465 and 09/561,074 entitled EPITOPE SYNCHRONIZATION IN ANTIGENPRESENTING CELLS, and METHOD OF EPITOPE DISCOVERY, respectively; both ofwhich were filed on Apr. 28, 2000, and which are both incorporatedherein by reference in their entireties.

[0015] Examples of housekeeping epitopes are disclosed in provisionalU.S. patent applications entitled EPITOPE SEQUENCES, No. 60/282,211,filed on Apr. 6, 2001; 60/337,017, filed on Nov. 7, 2001; 60/363,210filed Mar. 7, 2002; and 60/409,123, filed on Sep. 5, 2002; and U.S.application Ser. No. 10/117,937, filed on Apr. 4, 2002, which is alsoentitled EPITOPE SEQUENCES; which are all incorporated herein byreference in their entirety.

[0016] In other embodiments of the invention, the housekeepingepitope(s) can be flanked by arbitrary sequences or by sequencesincorporating residues known to be favored in immunoproteasome cleavagesites. As used herein the term “arbitrary sequences” refers to sequenceschosen without reference to the native sequence context of the epitope,their ability to promote processing, or immunological function. Infurther embodiments of the invention multiple epitopes can be arrayedhead-to-tail. These arrays can be made up entirely of housekeepingepitopes. Likewise, the arrays can include alternating housekeeping andimmune epitopes. Alternatively, the arrays can include housekeepingepitopes flanked by immune epitopes, whether complete or distallytruncated. Further, the arrays can be of any other similar arrangement.There is no restriction on placing a housekeeping epitope at theterminal positions of the array. The vectors can additionally containauthentic protein coding sequences or segments thereof containingepitope clusters as a source of immune epitopes. The term “authentic”refers to natural protein sequences.

[0017] Epitope clusters and their uses are described in U.S. patentapplication Ser. No. 09/561,571 entitled EPITOPE CLUSTERS, filed on Apr.28, 2000; Ser. No. 10/005,905, entitled EPITOPE SYNCHRONIZATION INANTIGEN PRESENTING CELLS, filed on Nov. 7, 2001; and Ser. No.10/026,066, filed on Dec. 7, 2001, also entitled EPITOPE SYNCHRONIZATIONIN ANTIGEN PRESENTING CELLS; all of which are incorporated herein byreference in their entirety.

[0018] Embodiments of the invention can encompass screening theconstructs to determine whether the housekeeping epitope is liberated.In constructs containing multiple housekeeping epitopes, embodiments caninclude screening to determine which epitopes are liberated. In apreferred embodiment, a vector containing an embedded epitope can beused to immunize HLA transgenic mice and the resultant CTL can be testedfor their ability to recognize target cells presenting the matureepitope. In another embodiment, target cells expressing immunoproteasomecan be transformed with the vector. The target cell may expressimmunoproteasome either constitutively, because of treatment withinterferon (IFN), or through genetic manipulation, for example. CTL thatrecognize the mature epitope can be tested for their ability torecognize these target cells. In yet another embodiment, the embeddedepitope can be prepared as a synthetic peptide. The synthetic peptidethen can be subjected to digestion by an immunoproteasome preparation invitro and the resultant fragments can be analyzed to determine the sitesof cleavage. Such polypeptides, recombinant or synthetic, from whichembedded epitopes can be successfully liberated, can also beincorporated into immunogenic compositions.

[0019] The invention disclosed herein relates to the identification of apolypeptide suitable for epitope liberation. One embodiment of theinvention, relates to a method of identifying a polypeptide suitable forepitope liberation including, for example, the steps of identifying anepitope of interest; providing a substrate polypeptide sequenceincluding the epitope, wherein the substrate polypeptide permitsprocessing by a proteasome; contacting the substrate polypeptide with acomposition including the proteasome, under conditions that supportprocessing of the substrate polypeptide by the proteasome; and assayingfor liberation of the epitope.

[0020] The epitope can be embedded in the substrate polypeptide, and insome aspects the substrate polypeptide can include more than oneepitope, for example. Also, the epitope can be a housekeeping epitope.

[0021] In one aspect, the substrate polypeptide can be a syntheticpeptide. Optionally, the substrate polypeptide can be included in aformulation promoting protein transfer. Alternatively, the substratepolypeptide can be a fusion protein. The fusion protein can furtherinclude a protein domain possessing protein transfer activity. Further,the contacting step can include immunization with the substratepolypeptide.

[0022] In another aspect, the substrate polypeptide can be encoded by apolynucleotide. The contacting step can include immunization with avector including the polynucleotide, for example. The immunization canbe carried out in an HLA-transgenic mouse or any other suitable animal,for example. Alternatively, the contacting step can include transforminga cell with a vector including the polynucleotide. In some embodimentsthe transformed cell can be a target cell that is targeted by CTL forpurposes of assaying for proper liberation of epitope.

[0023] The proteasome processing can take place intracellularly, eitherin vitro or in vivo. Further, the proteasome processing can take placein a cell-free system.

[0024] The assaying step can include a technique selected from the groupincluding, but not limited to, mass spectrometry, N-terminal poolsequencing, HPLC, and the like. Also, the assaying step can include a Tcell target recognition assay. The T cell target recognition assay canbe selected from the group including, but not limited to, a cytolyticactivity assay, a chromium release assay, a cytokine assay, an ELISPOTassay, tetramer analysis, and the like.

[0025] In still another aspect, the amino acid sequence of the substratepolypeptide including the epitope can be arbitrary. Also, the substratepolypeptide in which the epitope is embedded can be derived from anauthentic sequence of a target-associated antigen. Further, thesubstrate polypeptide in which the epitope is embedded can be conformedto a preferred immune proteasome cleavage site flanking sequence.

[0026] In another aspect, the substrate polypeptide can include an arrayof additional epitopes. Members of the array can be arrangedhead-to-tail, for example. The array can include more than onehousekeeping epitope. The more than one housekeeping epitope can includecopies of the same epitope. The array can include a housekeeping and animmune epitope, or alternating housekeeping and immune epitopes, forexample. Also, the array can include a housekeeping epitope positionedbetween two immune epitopes in an epitope battery. The array can includemultiple epitope batteries, so that there are two immune epitopesbetween each housekeeping epitope in the interior of the array.Optionally, at least one of the epitopes can be truncated distally toits junction with an adjacent epitope. The truncated epitopes can beimmune epitopes, for example. The truncated epitopes can have lengthsselected from the group including, but not limited to, 9, 8, 7, 6, 5, 4amino acids, and the like.

[0027] In still another aspect, the substrate polypeptide can include anarray of epitopes and epitope clusters. Members of the array can bearranged head-to-tail, for example.

[0028] In yet another aspect, the proteasome can be an immuneproteasome.

[0029] Another embodiment of the disclosed invention relates to vectorsincluding a housekeeping epitope expression cassette. The housekeepingepitope(s) can be derived from a target-associated antigen, and thehousekeeping epitope can be liberatable, that is capable of liberation,from a translation product of the cassette by immunoproteasomeprocessing.

[0030] In one aspect of the invention the expression cassette can encodean array of two or more epitopes or at least one epitope and at leastone epitope cluster. The members of the array can be arrangedhead-to-tail, for example. Also, the members of the array can bearranged head-to-tail separated by spacing sequences, for example.Further, the array can include a plurality of housekeeping epitopes. Theplurality of housekeeping epitopes can include more than one copy of thesame epitope or single copies of distinct epitopes, for example. Thearray can include at least one housekeeping epitope and at least oneimmune epitope. Also, the array can include alternating housekeeping andimmune epitopes. Further, the array includes a housekeeping epitopesandwiched between two immune epitopes so that there are two immuneepitopes between each housekeeping epitope in the interior of the array.The immune epitopes can be truncated distally to their junction with theadjacent housekeeping epitope.

[0031] In another aspect, the expression cassette further encodes anauthentic protein sequence, or segment thereof, including at least oneimmune epitope. Optionally, the segment can include at least one epitopecluster. The housekeeping epitope expression cassette and the authenticsequence including at least one immune epitope can be encoded in asingle reading frame or transcribed as a single mRNA species, forexample. Also, the housekeeping epitope expression cassette and theauthentic sequence including at least one immune epitope may not betranscribed as a single mRNA species.

[0032] In yet another aspect, the vector can include a DNA molecule oran RNA molecule. The vector can encode, for example, SEQ ID NO. 4, SEQID NO. 17, SEQ ID NO. 20, SEQ ID NO. 26, SEQ ID NO. 27, SEQ ID NO. 29,SEQ ID NO. 33, and the like. Also, the vector can include SEQ ID NO. 9,SEQ ID NO. 19, SEQ ID NO. 21, SEQ ID NO. 30, SEQ ID NO. 34, and thelike. Also, the vector can encode SEQ ID NO. 5 or SEQ ID NO. 18, forexample.

[0033] In still another aspect, the target-associated antigen can be anantigen derived from or associated with a tumor or an intracellularparasite, and the intracellular parasite can be, for example, a virus, abacterium, a protozoan, or the like.

[0034] Another embodiment of the invention relates to vectors includinga housekeeping epitope identified according to any of the methodsdisclosed herein, claimed or otherwise. For example, embodiments canrelate to vector encoding a substrate polypeptide that includes ahousekeeping epitope by any of the methods described herein.

[0035] In one aspect, the housekeeping epitope can be liberated from thecassette translation product by immune proteasome processing

[0036] Another embodiment of the disclosed invention relates to methodsof activating a T cell. The methods can include, for example, the stepsof contacting a vector including a housekeeping epitope expressioncassette with an APC. The housekeeping epitope can be derived from atarget-associated antigen, for example, and the housekeeping epitope canbe liberatable from a translation product of the cassette byimmunoproteasome processing. The methods can further include contactingthe APC with a T cell. The contacting of the vector with the APC canoccur in vitro or in vivo.

[0037] Another embodiment of the disclosed invention relates to asubstrate polypeptide including a housekeeping epitope wherein thehousekeeping epitope can be liberated by immunoproteasome processing ina pAPC.

[0038] Another embodiment of the disclosed invention relates to a methodof activating a T cell comprising contacting a substrate polypeptideincluding a housekeeping epitope with an APC wherein the housekeepingepitope can be liberated by immunoproteasome processing and contactingthe APC with a T cell.

BRIEF DESCRIPTION OF THE DRAWINGS

[0039]FIG. 1 depicts the sequence of Melan-A (SEQ ID NO: 2), showingclustering of class I HLA epitopes.

[0040]FIG. 2 depicts the sequence of SSX-2 (SEQ ID NO: 40), showingclustering of class I HLA epitopes.

[0041]FIG. 3 depicts the sequence of NY-ESO (SEQ ID NO: 11), showingclustering of class I HLA epitopes.

[0042]FIG. 4. An illustrative drawing depicting pMA2M.

[0043]FIG. 5. Assay results showing the % of specific lysis ofELAGIGILTV pulsed and unpulsed T2 target cells by mock immunized CTL.

[0044]FIG. 6. Assay results showing the % of specific lysis ofELAGIGILTV pulsed and unpulsed T2 target cells by pVAXM3 immunized CTL.

[0045]FIG. 7. Assay results showing the % of specific lysis ofELAGIGILTV pulsed and unpulsed T2 target cells by pVAXM2 immunized CTL.

[0046]FIG. 8. Assay results showing the % of specific lysis ofELAGIGILTV pulsed and unpulsed T2 target cells by pVAXM1 immunized CTL.

[0047]FIG. 9. Illustrates a sequence of SEQ ID NO. 22 from which theNY-ESO-1₁₅₇₋₁₆₅ epitope is liberated by immunoproteasomal processing.

[0048]FIG. 10. Shows the differential processing by immunoproteasome andhousekeeping proteasome of the SLLMWITQC epitope (SEQ ID NO. 12) in itsnative context where the cleavage following the C is more efficientlyproduced by housekeeping than immunoproteasome.

[0049]FIG. 11. 8A: Shows the results of the human immunoproteasomedigest of SEQ ID NO. 31. 8B: Shows the comparative results of mouseversus human immunoproteasome digestion of SEQ ID NO. 31.

[0050]FIG. 12. Shows the differential processing of SSX-2₃₁₋₆₈ byhousekeeping and immunoproteasome.

DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENT

[0051] Definitions

[0052] Unless otherwise clear from the context of the use of a termherein, the following listed terms shall generally have the indicatedmeanings for purposes of this description.

[0053] PROFESSIONAL ANTIGEN-PRESENTING CELL (PAPC)—a cell that possessesT cell costimulatory molecules and is able to induce a T cell response.Well characterized pAPCs include dendritic cells, B cells, andmacrophages.

[0054] PERIPHERAL CELL—a cell that is not a pAPC.

[0055] HOUSEKEEPING PROTEASOME—a proteasome normally active inperipheral cells, and generally not present or not strongly active inpAPCs.

[0056] IMMUNOPROTEASOME—a proteasome normally active in pAPCs; theimmunoproteasome is also active in some peripheral cells in infectedtissues or following exposure to interferon.

[0057] EPITOPE—a molecule or substance capable of stimulating an immuneresponse. In preferred embodiments, epitopes according to thisdefinition include but are not necessarily limited to a polypeptide anda nucleic acid encoding a polypeptide, wherein the polypeptide iscapable of stimulating an immune response. In other preferredembodiments, epitopes according to this definition include but are notnecessarily limited to peptides presented on the surface of cells, thepeptides being non-covalently bound to the binding cleft of class I MHC,such that they can interact with T cell receptors (TCR). Epitopespresented by class I MHC may be in immature or mature form. “Mature”refers to an MHC epitope in distinction to any precursor (“immature”)that may include or consist essentially of a housekeeping epitope, butalso includes other sequences in a primary translation product that areremoved by processing, including without limitation, alone or in anycombination, proteasomal digestion, N-terminal trimming, or the actionof exogenous enzymatic activities. Thus, a mature epitope may beprovided embedded in a somewhat longer polypeptide, the immunologicalpotential of which is due, at least in part, to the embedded epitope; orin its ultimate form that can bind in the MHC binding cleft to berecognized by TCR, respectively.

[0058] MHC EPITOPE—a polypeptide having a known or predicted bindingaffinity for a mammalian class I or class II major histocompatibilitycomplex (MHC) molecule.

[0059] HOUSEKEEPING EPITOPE—In a preferred embodiment, a housekeepingepitope is defined as a polypeptide fragment that is an MHC epitope, andthat is displayed on a cell in which housekeeping proteasomes arepredominantly active. In another preferred embodiment, a housekeepingepitope is defined as a polypeptide containing a housekeeping epitopeaccording to the foregoing definition, that is flanked by one to severaladditional amino acids. In another preferred embodiment, a housekeepingepitope is defined as a nucleic acid that encodes a housekeeping epitopeaccording to the foregoing definitions. Exemplary housekeeping epitopesare provide in U.S. application Ser. No. 10/117,937, filed on Apr. 4,2002; and U.S. Provisional Application No. 60/282,211, filed on Apr. 6,2001; 60/337,017, filed on Nov. 7, 2001; 60/363,210 filed Mar. 7, 2002;and 60/409,123, filed on Sep. 5, 2002; all of which are entitled EPITOPESEQUENCES, and all of which above were incorporated herein by referencein their entireties.

[0060] IMMUNE EPITOPE—In a preferred embodiment, an immune epitope isdefined as a polypeptide fragment that is an MHC epitope, and that isdisplayed on a cell in which immunoproteasomes are predominantly active.In another preferred embodiment, an immune epitope is defined as apolypeptide containing an immune epitope according to the foregoingdefinition, that is flanked by one to several additional amino acids. Inanother preferred embodiment, an immune epitope is defined as apolypeptide including an epitope cluster sequence, having at least twopolypeptide sequences having a known or predicted affinity for a class IMHC. In yet another preferred embodiment, an immune epitope is definedas a nucleic acid that encodes an immune epitope according to any of theforegoing definitions.

[0061] TARGET CELL—a cell to be targeted by the vaccines and methods ofthe invention. Examples of target cells according to this definitioninclude but are not necessarily limited to: a neoplastic cell and a cellharboring an intracellular parasite, such as, for example, a virus, abacterium, or a protozoan. Target cells can also include cells that aretargeted by CTL as a part of assays to determine or confirm properepitope liberation and processing by a cell expressing immunoproteasome,to determine T cell specificity or immunogenicity for a desired epitope.Such cells may be transfored to express the substrate or liberationsequence, or the cells can simply be pulsed with peptide/epitope.

[0062] TARGET-ASSOCIATED ANTIGEN (TAA)—a protein or polypeptide presentin a target cell.

[0063] TUMOR-ASSOCIATED ANTIGENS (TuAA)—a TAA, wherein the target cellis a neoplastic cell.

[0064] HLA EPITOPE—a polypeptide having a known or predicted bindingaffinity for a human class I or class II HLA complex molecule.

[0065] ANTIBODY—a natural immunoglobulin (Ig), poly- or monoclonal, orany molecule composed in whole or in part of an Ig binding domain,whether derived biochemically or by use of recombinant DNA. Examplesinclude inter alia, F(ab), single chain Fv, and Ig variable region-phagecoat protein fusions.

[0066] ENCODE—an open-ended term such that a nucleic acid encoding aparticular amino acid sequence can consist of codons specifying that(poly)peptide, but can also comprise additional sequences eithertranslatable, or for the control of transcription, translation, orreplication, or to facilitate manipulation of some host nucleic acidconstruct.

[0067] SUBSTANTIAL SIMILARITY—this term is used to refer to sequencesthat differ from a reference sequence in an inconsequential way asjudged by examination of the sequence. Nucleic acid sequences encodingthe same amino acid sequence are substantially similar despitedifferences in degenerate positions or modest differences in length orcomposition of any non-coding regions. Amino acid sequences differingonly by conservative substitution or minor length variations aresubstantially similar. Additionally, amino acid sequences comprisinghousekeeping epitopes that differ in the number of N-terminal flankingresidues, or immune epitopes and epitope clusters that differ in thenumber of flanking residues at either terminus, are substantiallysimilar. Nucleic acids that encode substantially similar amino acidsequences are themselves also substantially similar.

[0068] FUNCTIONAL SIMILARITY—this term is used to refer to sequencesthat differ from a reference sequence in an inconsequential way asjudged by examination of a biological or biochemical property, althoughthe sequences may not be substantially similar. For example, two nucleicacids can be useful as hybridization probes for the same sequence butencode differing amino acid sequences. Two peptides that inducecross-reactive CTL responses are functionally similar even if theydiffer by non-conservative amino acid substitutions (and thus do notmeet the substantial similarity definition). Pairs of antibodies, orTCRs, that recognize the same epitope can be functionally similar toeach other despite whatever structural differences exist. In testing forfunctional similarity of immunogenicity one would generally immunizewith the “altered” antigen and test the ability of the elicited response(Ab, CTL, cytokine production, etc.) to recognize the target antigen.Accordingly, two sequences may be designed to differ in certain respectswhile retaining the same function. Such designed sequence variants areamong the embodiments of the present invention.

[0069] EXPRESSION CASSETTE—a polynucleotide sequence encoding apolypeptide, operably linked to a promoter and other transcription andtranslation control elements, including but not limited to enhancers,termination codons, internal ribosome entry sites, and polyadenylationsites. The cassette can also include sequences that facilitate moving itfrom one host molecule to another.

[0070] EMBEDDED EPITOPE—an epitope contained within a longerpolypeptide, also can include an epitope in which either the N-terminusor the C-terminus is embedded such that the epitope is not in aninterior position.

[0071] MATURE EPITOPE—a peptide with no additional sequence beyond thatpresent when the epitope is bound in the MHC peptide-binding cleft.

[0072] EPITOPE CLUSTER—a polypeptide, or a nucleic acid sequenceencoding it, that is a segment of a native protein sequence comprisingtwo or more known or predicted epitopes with binding affinity for ashared MHC restriction element, wherein the density of epitopes withinthe cluster is greater than the density of all known or predictedepitopes with binding affinity for the shared MHC restriction elementwithin the complete protein sequence, and as disclosed in U.S. patentapplication Ser. No. 09/561,571 entitled EPITOPE CLUSTERS.

[0073] SUBSTRATE OR LIBERATION SEQUENCE—a designed or engineeredsequence comprising or encoding a housekeeping epitope (according to thefirst of the definitions offered above) embedded in a larger sequencethat provides a context allowing the housekeeping epitope to beliberated by immunoproteasomal processing, directly or in combinationwith N-terminal trimming or other processes.

[0074] Epitope Clusters

[0075] Embodiments of the invention disclosed herein provide epitopecluster regions (ECRs) for use in vaccines and in vaccine design andepitope discovery. Specifically, embodiments of the invention relate toidentifying epitope clusters for use in generating immunologicallyactive compositions directed against target cell populations, and foruse in the discovery of discrete housekeeping epitopes and immuneepitopes. In many cases, numerous putative class I MHC epitopes mayexist in a single target-associated antigen (TAA). Such putativeepitopes are often found in clusters (ECRs), MHC epitopes distributed ata relatively high density within certain regions in the amino acidsequence of the parent TAA. Since these ECRs include multiple putativeepitopes with potential useful biological activity in inducing an immuneresponse, they represent an excellent material for in vitro or in vivoanalysis to identify particularly useful epitopes for vaccine design.And, since the epitope clusters can themselves be processed inside acell to produce active MHC epitopes, the clusters can be used directlyin vaccines, with one or more putative epitopes in the cluster actuallybeing processed into an active MHC epitope.

[0076] The use of ECRs in vaccines offers important technologicaladvances in the manufacture of recombinant vaccines, and further offerscrucial advantages in safety over existing nucleic acid vaccines thatencode whole protein sequences. Recombinant vaccines generally rely onexpensive and technically challenging production of whole proteins inmicrobial fermentors. ECRs offer the option of using chemicallysynthesized polypeptides, greatly simplifying development andmanufacture, and obviating a variety of safety concerns. Similarly, theability to use nucleic acid sequences encoding ECRs, which are typicallyrelatively short regions of an entire sequence, allows the use ofsynthetic oligonucleotide chemistry processes in the development andmanipulation of nucleic acid based vaccines, rather than the moreexpensive, time consuming, and potentially difficult molecular biologyprocedures involved with using whole gene sequences.

[0077] Since an ECR is encoded by a nucleic acid sequence that isrelatively short compared to that which encodes the whole protein fromwhich the ECR is found, this can greatly improve the safety of nucleicacid vaccines. An important issue in the field of nucleic acid vaccinesis the fact that the extent of sequence homology of the vaccine withsequences in the animal to which it is administered determines theprobability of integration of the vaccine sequence into the genome ofthe animal. A fundamental safety concern of nucleic acid vaccines istheir potential to integrate into genomic sequences, which can causederegulation of gene expression and tumor transformation. The Food andDrug Administration has advised that nucleic acid and recombinantvaccines should contain as little sequence homology with human sequencesas possible. In the case of vaccines delivering tumor-associatedantigens, it is inevitable that the vaccines contain nucleic acidsequences that are homologous to those which encode proteins that areexpressed in the tumor cells of patients. It is, however, highlydesirable to limit the extent of those sequences to that which isminimally essential to facilitate the expression of epitopes forinducing therapeutic immune responses. The use of ECRs thus offers thedual benefit of providing a minimal region of homology, whileincorporating multiple epitopes that have potential therapeutic value.

[0078] Note that the following discussion sets forth the inventors'understanding of the operation of the invention. However, it is notintended that this discussion limit the patent to any particular theoryof operation not set forth in the claims.

[0079] ECRs are Processed into MHC-Binding Epitopes in pAPCs

[0080] The immune system constantly surveys the body for the presence offoreign antigens, in part through the activity of pAPCs. The pAPCsendocytose matter found in the extracellular milieu, process that matterfrom a polypeptide form into shorter oligopeptides of about 3 to 23amino acids in length, and display some of the resulting peptides to Tcells via the MHC complex of the pAPCs. For example, a tumor cell uponlysis releases its cellular contents, including various proteins, intothe extracellular milieu. Those released proteins can be endocytosed bypAPCs and processed into discrete peptides that are then displayed onthe surface of the pAPCs via the MHC. By this mechanism, it is not theentire target protein that is presented on the surface of the pAPCs, butrather only one or more discrete fragments of that protein that arepresented as MHC-binding epitopes. If a presented epitope is recognizedby a T cell, that T cell is activated and an immune response results.

[0081] Similarly, the scavenger receptors on pAPC can take-up nakednucleic acid sequences or recombinant organisms containing targetnucleic acid sequences. Uptake of the nucleic acid sequences into thepAPC subsequently results in the expression of the encoded products. Asabove, when an ECR can be processed into one or more useful epitopes,these products can be presented as MHC epitopes for recognition by Tcells.

[0082] MHC-binding epitopes are often distributed unevenly throughout aprotein sequence in clusters. Embodiments of the invention are directedto identifying epitope cluster regions (ECRs) in a particular region ofa target protein. Candidate ECRs are likely to be natural substrates forvarious proteolytic enzymes and are likely to be processed into one ormore epitopes for MHC display on the surface of an pAPC. In contrast tomore traditional vaccines that deliver whole proteins or biologicalagents, ECRs can be administered as vaccines, resulting in a highprobability that at least one epitope will be presented on MHC withoutrequiring the use of a full length sequence.

[0083] The Use of ECRs in Identifying Discrete MHC-Binding Epitopes

[0084] Identifying putative MHC epitopes for use in vaccines oftenincludes the use of available predictive algorithms that analyze thesequences of proteins or genes to predict binding affinity of peptidefragments for MHC. These algorithms rank putative epitopes according topredicted affinity or other characteristics associated with MHC binding.Exemplary algorithms for this kind of analysis include the Rammensee andNIH (Parker) algorithms. However, identifying epitopes that arenaturally present on the surface of cells from among putative epitopespredicted using these algorithms has proven to be a difficult andlaborious process. The use of ECRs in an epitope identification processcan enormously simplify the task of identifying discrete MHC bindingepitopes.

[0085] In a preferred embodiment, ECR polypeptides are synthesized on anautomated peptide synthesizer and these ECRs are then subjected to invitro digests using proteolytic enzymes involved in processing proteinsfor presentation of the epitopes. Mass spectrometry and/or analyticalHPLC are then used to identify the digest products and in vitro MHCbinding studies are used to assess the ability of these products toactually bind to MHC. Once epitopes contained in ECRs have been shown tobind MHC, they can be incorporated into vaccines or used as diagnostics,either as discrete epitopes or in the context of ECRs.

[0086] The use of an ECR (which because of its relatively short sequencecan be produced through chemical synthesis) in this preferred embodimentis a significant improvement over what otherwise would require the useof whole protein. This is because whole proteins have to be producedusing recombinant expression vector systems and/or complex purificationprocedures. The simplicity of using chemically synthesized ECRs enablesthe analysis and identification of large numbers of epitopes, whilegreatly reducing the time and expense of the process as compared toother currently used methods. The use of a defined ECR also greatlysimplifies mass spectrum analysis of the digest, since the products ofan ECR digest are a small fraction of the digest products of a wholeprotein.

[0087] In another embodiment, nucleic acid sequences encoding ECRs areused to express the polypeptides in cells or cell lines to assess whichepitopes are presented on the surface. A variety of means can be used todetect the epitope on the surface. Preferred embodiments involve thelysis of the cells and affinity purification of the MHC, and subsequentelution and analysis of peptides from the MHC; or elution of epitopesfrom intact cells; (Falk, K. et al. Nature 351:290, 1991, and U.S. Pat.No. 5,989,565, respectively, both of which references are incorporatedherein by reference in their entirety). A sensitive method for analyzingpeptides eluted in this way from the MHC employs capillary ornanocapillary HPLC ESI mass spectrometry and on-line sequencing.

[0088] Target-Associated Antigens that Contain ECRs

[0089] TAAs from which ECRs may be defined include those from TuAAs,including oncofetal, cancer-testis, deregulated genes, fusion genes fromerrant translocations, differentiation antigens, embryonic antigens,cell cycle proteins, mutated tumor suppressor genes, and overexpressedgene products, including oncogenes. In addition, ECRs may be derivedfrom virus gene products, particularly those associated with virusesthat cause chronic diseases or are oncogenic, such as the herpesviruses, human papilloma viruses, human immunodeficiency virus, andhuman T cell leukemia virus. Also ECRs may be derived from gene productsof parasitic organisms, such as Trypanosoma, Leishmania, and otherintracellular or parasitic organisms.

[0090] Some of these TuAA include α-fetoprotein, carcinoembryonicantigen (CEA), esophageal cancer derived NY-ESO-1, and SSX genes, SCP-1,PRAME, MART-1/MelanA (MART-1), gp100 (Pmel 17), tyrosinase, TRP-1,TRP-2, MAGE-1, MAGE-2, MAGE-3, BAGE, GAGE-1, GAGE-2, p15; overexpressedoncogenes and mutated tumor-suppressor genes such as p53, Ras,HER-2/neu; unique tumor antigens resulting from chromosomaltranslocations such as BCR-ABL, E2A-PRL, H4-RET, IGH-IGK, MYL-RAR1 andviral antigens, EBNA1, EBNA2, HPV-E6, -E7; prostate specific antigen(PSA), prostate stem cell antigen (PSCA), MAAT-1, GP-100, TSP-180,MAGE-4, MAGE-5, MAGE-6, RAGE, p185erbB-2, p185erbB-3, c-met, nm-23H1,TAG-72, CA 19-9, CA 72-4, CAM 17.1, NuMa, K-ras, β-Catenin, CDK4, Mum-1,p15, and p16.

[0091] Numerous other TAAs are also contemplated for both pathogens andtumors. In terms of TuAAs, a variety of methods are available and wellknown in the art to identify genes and gene products that aredifferentially expressed in neoplastic cells as compared to normalcells. Examples of these techniques include differential hybridization,including the use of microarrays; subtractive hybridization cloning;differential display, either at the level of mRNA or protein expression;EST sequencing; and SAGE (sequential analysis of gene expression). Thesenucleic acid techniques have been reviewed by Carulli, J. P. et al., J.Cellular Biochem Suppl. 30/31:286-296, 1998 (hereby incorporated byreference). Differential display of proteins involves, for example,comparison of two-dimensional polyacrylamide gel electrophoresis of celllysates from tumor and normal tissue, location of protein spots uniqueor overexpressed in the tumor, recovery of the protein from the gel, andidentification of the protein using traditional biochemical- or massspectrometry-based sequencing. An additional technique foridentification of TAAs is the Serex technique, discussed in Türeci, Ö.,Sahin, U., and Pfreundschuh, M., “Serological analysis of human tumorantigens: molecular definition and implications”, Molecular MedicineToday, 3:342, 1997, and hereby incorporated by reference.

[0092] Use of these and other methods provides one of skill in the artthe techniques necessary to identify genes and gene products containedwithin a target cell that may be used as potential candidate proteinsfor generating the epitopes of the invention disclosed. However, it isnot necessary, in practicing the invention, to identify a novel TuAA orTAA. Rather, embodiments of the invention make it possible to identifyECRs from any relevant protein sequence, whether the sequence is alreadyknown or is new.

[0093] Protein Sequence Analysis to Identify Epitope Clusters

[0094] In preferred embodiments of the invention, identification of ECRsinvolves two main steps: (1) identifying good putative epitopes; and (2)defining the limits of any clusters in which these putative epitopes arelocated. There are various preferred embodiments of each of these twosteps, and a selected embodiment for the first step can be freelycombined with a selected embodiment for the second step. The methods andembodiments that are disclosed herein for each of these steps are merelyexemplary, and are not intended to limit the scope of the invention inany way. Persons of skill in the art will appreciate the specific toolsthat can be applied to the analysis of a specific TAA, and such analysiscan be conducted in numerous ways in accordance with the invention.

[0095] Preferred embodiments for identifying good putative epitopesinclude the use of any available predictive algorithm that analyzes thesequences of proteins or genes to predict binding affinity of peptidefragments for MHC, or to rank putative epitopes according to predictedaffinity or other characteristics associated with MHC binding. Asdescribed above, available exemplary algorithms for this kind ofanalysis include the Rammensee and NIH (Parker) algorithms. Likewise,good putative epitopes can be identified by direct or indirect assays ofMHC binding. To choose “good” putative epitopes, it is necessary to seta cutoff point in terms of the score reported by the prediction softwareor in terms of the assayed binding affinity. In some embodiments, such acutoff is absolute. For example, the cutoff can be based on the measuredor predicted half time of dissociation between an epitope and a selectedMHC allele. In such cases, embodiments of the cutoff can be any halftime of dissociation longer than, for example, 0.5 minutes; in apreferred embodiment longer than 2.5 minutes; in a more preferredembodiment longer than 5 minutes; and in a highly stringent embodimentcan be longer than 10, or 20, or 25 minutes. In these embodiments, thegood putative epitopes are those that are predicted or identified tohave good MHC binding characteristics, defined as being on the desirableside of the designated cutoff point. Likewise, the cutoff can be basedon the measured or predicted binding affinity between an epitope and aselected MHC allele. Additionally, the absolute cutoff can be simply aselected number of putative epitopes.

[0096] In other embodiments, the cutoff is relative. For example, aselected percentage of the total number of putative epitopes can be usedto establish the cutoff for defining a candidate sequence as a goodputative epitope. Again the properties for ranking the epitopes arederived from measured or predicted MHC binding; the property used forsuch a determination can be any that is relevant to or indicative ofbinding. In preferred embodiments, identification of good putativeepitopes can combine multiple methods of ranking candidate sequences. Insuch embodiments, the good epitopes are typically those that eitherrepresent a consensus of the good epitopes based on different methodsand parameters, or that are particularly highly ranked by at least oneof the methods.

[0097] When several good putative epitopes have been identified, theirpositions relative to each other can be analyzed to determine theoptimal clusters for use in vaccines or in vaccine design. This analysisis based on the density of a selected epitope characteristic within thesequence of the TAA. The regions with the highest density of thecharacteristic, or with a density above a certain selected cutoff, aredesignated as ECRs. Various embodiments of the invention employdifferent characteristics for the density analysis. For example, onepreferred characteristic is simply the presence of any good putativeepitope (as defined by any appropriate method). In this embodiment, allputative epitopes above the cutoff are treated equally in the densityanalysis, and the best clusters are those with the highest density ofgood putative epitopes per amino acid residue. In another embodiment,the preferred characteristic is based on the parameter(s) previouslyused to score or rank the putative epitopes. In this embodiment, aputative epitope with a score that is twice as high as another putativeepitope is doubly weighted in the density analysis, relative to theother putative epitope. Still other embodiments take the score or rankinto account, but on a diminished scale, such as, for example, by usingthe log or the square root of the score to give more weight to someputative epitopes than to others in the density analysis.

[0098] Depending on the length of the TAA to be analyzed, the number ofpossible candidate epitopes, the number of good putative epitopes, thevariability of the scoring of the good putative epitopes, and otherfactors that become evident in any given analysis, the variousembodiments of the invention can be used alone or in combination toidentify those ECRs that are most useful for a given application.Iterative or parallel analyses employing multiple approaches can bebeneficial in many cases. ECRs are tools for increased efficiency ofidentifying true MHC epitopes, and for efficient “packaging” of MHCepitopes into vaccines. Accordingly, any of the embodiments describedherein, or other embodiments that are evident to those of skill in theart based on this disclosure, are useful in enhancing the efficiency ofthese efforts by using ECRs instead of using complete TAAs in vaccinesand vaccine design.

[0099] Since many or most TAAs have regions with low density ofpredicted MHC epitopes, using ECRs provides a valuable methodology thatavoids the inefficiencies of including regions of low epitope density invaccines and in epitope identification protocols. Thus, useful ECRs canalso be defined as any portion of a TAA that is not the whole TAA,wherein the portion has a higher density of putative epitopes than thewhole TAA, or than any regions of the TAA that have a particularly lowdensity of putative epitopes. In this aspect of the invention,therefore, an ECR can be any fragment of a TAA with elevated epitopedensity. In some embodiments, an ECR can include a region up to about80% of the length of the TAA. In a preferred embodiment, an ECR caninclude a region up to about 50% of the length of the TAA. In a morepreferred embodiment, an ECR can include a region up to about 30% of thelength of the TAA. And in a most preferred embodiment, an ECR caninclude a region of between 5 and 15% of the length of the TAA.

[0100] In another aspect of the invention, the ECR can be defined interms of its absolute length. Accordingly, by this definition, theminimal cluster for 9-mer epitopes includes 10 amino acid residues andhas two overlapping 9-mers with 8 amino acids in common. In a preferredembodiment, the cluster is between about 15 and 75 amino acids inlength. In a more preferred embodiment, the cluster is between about 20and 60 amino acids in length. In a most preferred embodiment, thecluster is between about 30 and 40 amino acids in length.

[0101] In practice, as described above, ECR identification can employ asimple density function such as the number of epitopes divided by thenumber of amino acids spanned by the those epitopes. It is notnecessarily required that the epitopes overlap, but the value for asingle epitope is not significant. If only a single value for apercentage cutoff is used and an absolute cutoff in the epitopeprediction is not used, it is possible to set a single threshold at thisstep to define a cluster. However, using both an absolute cutoff andcarrying out the first step using different percentage cutoffs, canproduce variations in the global density of candidate epitopes. Suchvariations can require further accounting or manipulation. For example,an overlap of 2 epitopes is more significant if only 3 candidateepitopes were considered, than if 30 candidates were considered for anyparticular length protein. To take this feature into consideration, theweight given to a particular cluster can further be divided by thefraction of possible peptides actually being considered, in order toincrease the significance of the calculation. This scales the result tothe average density of predicted epitopes in the parent protein.

[0102] Similarly, some embodiments base the scoring of good putativeepitopes on the average number of peptides considered per amino acid inthe protein. The resulting ratio represents the factor by which thedensity of predicted epitopes in the putative cluster differs from theaverage density in the protein. Accordingly, an ECR is defined in oneembodiment as any region containing two or more predicted epitopes forwhich this ratio exceeds 2, that is, any region with twice the averagedensity of epitopes. In other embodiments, the region is defined as anECR if the ratio exceeds 1.5, 3, 4, or 5, or more.

[0103] Considering the average number of peptides per amino acid in atarget protein to calculate the presence of an ECR highlights denselypopulated ECRs without regard to the score/affinity of the individualconstituents. This is most appropriate for use of score-based cutoffs.However, an ECR with only a small number of highly ranked candidates canbe of more biological significance than a cluster with several denselypacked but lower ranking candidates, particularly if only a smallpercentage of the total number of candidate peptides were designated asgood putative epitopes. Thus in some embodiments it is appropriate totake into consideration the scores of the individual peptides. This ismost readily accomplished by substituting the sum of the scores of thepeptides in the putative cluster for the number of peptides in theputative cluster in the calculation described above.

[0104] This sum of scores method is more sensitive to sparsely populatedclusters containing high scoring epitopes. Because the wide range ofscores (i.e. half times of dissociation) produced by theBIMAS-NIH/Parker algorithm can lead to a single high scoring peptidedwarfing the contribution of other potential epitopes, the log of thescore rather than the score itself is preferably used in this procedure.

[0105] Various other calculations can be devised under one or anothercondition. Generally speaking, the epitope density function isconstructed so that it is proportional to the number of predictedepitopes, their scores, their ranks, and the like, within the putativecluster, and inversely proportional to the number of amino acids orfraction of protein contained within that putative cluster.Alternatively, the function can be evaluated for a window of a selectednumber of contiguous amino acids. In either case the function is alsoevaluated for all predicted epitopes in the whole protein. If the ratioof values for the putative cluster (or window) and the whole protein isgreater than, for example, 1.5, 2, 3, 4, 5, or more, an ECR is defined.

[0106] Analysis of Target Gene Products for MHC Binding

[0107] Once a TAA has been identified, the protein sequence can be usedto identify putative epitopes with known or predicted affinity to theMHC peptide binding cleft. Tests of peptide fragments can be conductedin vitro, or using the sequence can be computer analyzed to determineMHC receptor binding of the peptide fragments. In one embodiment of theinvention, peptide fragments based on the amino acid sequence of thetarget protein are analyzed for their predicted ability to bind to theMHC peptide binding cleft. Examples of suitable computer algorithms forthis purpose include that found at the world wide web page of Hans-GeorgRammensee, Jutta Bachmann, Niels Emmerich, Stefan Stevanovic: SYFPEITHI:An Internet Database for MHC Ligands and Peptide Motifs (access viahypertext transfer protocol://134.2.96.221/scripts/hlaserver.dll/EpPredict.htm). Results obtainedfrom this method are discussed in Rammensee, et al., “MHC Ligands andPeptide Motifs,” Landes Bioscience Austin, Tex., 224-227, 1997, which ishereby incorporated by reference in its entirety. Another site ofinterest is found at hypertext transfer protocol://bimas.dcrt.nih.gov/molbio/hla_bind, which also contains a suitablealgorithm. The methods of this web site are discussed in Parker, et al.,“Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side-chains,” J. Immunol.152:163-175, which is hereby incorporated by reference in its entirety.

[0108] As an alternative to predictive algorithms, a number of standardin vitro receptor binding affinity assays are available to identifypeptides having an affinity for a particular allele of MHC. Accordingly,by the method of this aspect of the invention, the initial population ofpeptide fragments can be narrowed to include only putative epitopeshaving an actual or predicted affinity for the selected allele of MHC.Selected common alleles of MHC I, and their approximate frequencies, arereported in the tables below. TABLE 1 Estimated gene frequencies ofHLA-A antigens CAU AFR ASI LAT NAT Antigen Gf^(a) SE^(b) Gf SE Gf SE GfSE Gf SE A1 15.1843 0.0489 5.7256 0.0771 4.4818 0.0846 7.4007 0.097812.0316 0.2533 A2 28.6535 0.0619 18.8849 0.1317 24.6352 0.1794 28.11980.1700 29.3408 0.3585 A3 13.3890 0.0463 8.4406 0.0925 2.6454 0.06558.0789 0.1019 11.0293 0.2437 A28 4.4652 0.0280 9.9269 0.0997 1.76570.0537 8.9446 0.1067 5.3856 0.1750 A36 0.0221 0.0020 1.8836 0.04480.0148 0.0049 0.1584 0.0148 0.1545 0.0303 A23 1.8287 0.0181 10.20860.1010 0.3256 0.0231 2.9269 0.0628 1.9903 0.1080 A24 9.3251 0.03952.9668 0.0560 22.0391 0.1722 13.2610 0.1271 12.6613 0.2590 A9 unsplit0.0809 0.0038 0.0367 0.0063 0.0858 0.0119 0.0537 0.0086 0.0356 0.0145 A9total 11.2347 0.0429 13.2121 0.1128 22.4505 0.1733 16.2416 0.138214.6872 0.2756 A25 2.1157 0.0195 0.4329 0.0216 0.0990 0.0128 1.19370.0404 1.4520 0.0924 A26 3.8795 0.0262 2.8284 0.0547 4.6628 0.08623.2612 0.0662 2.4292 0.1191 A34 0.1508 0.0052 3.5228 0.0610 1.35290.0470 0.4928 0.0260 0.3150 0.0432 A43 0.0018 0.0006 0.0334 0.00600.0231 0.0062 0.0055 0.0028 0.0059 0.0059 A66 0.0173 0.0018 0.22330.0155 0.0478 0.0089 0.0399 0.0074 0.0534 0.0178 A10 unsplit 0.07900.0038 0.0939 0.0101 0.1255 0.0144 0.0647 0.0094 0.0298 0.0133 A10 total6.2441 0.0328 7.1348 0.0850 6.3111 0.0993 5.0578 0.0816 4.2853 0.1565A29 3.5796 0.0252 3.2071 0.0582 1.1233 0.0429 4.5156 0.0774 3.43450.1410 A30 2.5067 0.0212 13.0969 0.1129 2.2025 0.0598 4.4873 0.07722.5314 0.1215 A31 2.7386 0.0221 1.6556 0.0420 3.6005 0.0761 4.83280.0800 6.0881 0.1855 A32 3.6956 0.0256 1.5384 0.0405 1.0331 0.04112.7064 0.0604 2.5521 0.1220 A33 1.2080 0.0148 6.5607 0.0822 9.27010.1191 2.6593 0.0599 1.0754 0.0796 A74 0.0277 0.0022 1.9949 0.04610.0561 0.0096 0.2027 0.0167 0.1068 0.0252 A19 unsplit 0.0567 0.00320.2057 0.0149 0.0990 0.0128 0.1211 0.0129 0.0475 0.0168 A19 total13.8129 0.0468 28.2593 0.1504 17.3846 0.1555 19.5252 0.1481 15.83580.2832 AX 0.8204 0.0297 4.9506 0.0963 2.9916 0.1177 1.6332 0.0878 1.84540.1925

[0109] TABLE 2 Estimated gene frequencies for HLA-B antigens CAU AFR ASILAT NAT Antigen Gf^(a) SE^(b) Gf SE Gf SE Gf SE Gf SE B7 12.1782 0.044510.5960 0.1024 4.2691 0.0827 6.4477 0.0918 10.9845 0.2432 B8 9.40770.0397 3.8315 0.0634 1.3322 0.0467 3.8225 0.0715  8.5789 0.2176 B132.3061 0.0203 0.8103 0.0295 4.9222 0.0886 1.2699 0.0416  1.7495 0.1013B14 4.3481 0.0277 3.0331 0.0566 0.5004 0.0287 5.4166 0.0846  2.98230.1316 B18 4.7980 0.0290 3.2057 0.0582 1.1246 0.0429 4.2349 0.0752 3.3422 0.1391 B27 4.3831 0.0278 1.2918 0.0372 2.2355 0.0603 2.37240.0567  5.1970 0.1721 B35 9.6614 0.0402 8.5172 0.0927 8.1203 0.112214.6516 0.1329 10.1198 0.2345 B37 1.4032 0.0159 0.5916 0.0252 1.23270.0449 0.7807 0.0327  0.9755 0.0759 B41 0.9211 0.0129 0.8183 0.02960.1303 0.0147 1.2818 0.0418  0.4766 0.0531 B42 0.0608 0.0033 5.69910.0768 0.0841 0.0118 0.5866 0.0284  0.2856 0.0411 B46 0.0099 0.00130.0151 0.0040 4.9292 0.0886 0.0234 0.0057  0.0238 0.0119 B47 0.20690.0061 0.1305 0.0119 0.0956 0.0126 0.1832 0.0159  0.2139 0.0356 B480.0865 0.0040 0.1316 0.0119 2.0276 0.0575 1.5915 0.0466  1.0267 0.0778B53 0.4620 0.0092 10.9529 0.1039 0.4315 0.0266 1.6982 0.0481  1.08040.0798 B59 0.0020 0.0006 0.0032 0.0019 0.4277 0.0265 0.0055 0.0028 0^(c) — B67 0.0040 0.0009 0.0086 0.0030 0.2276 0.0194 0.0055 0.0028 0.0059 0.0059 B70 0.3270 0.0077 7.3571 0.0866 0.8901 0.0382 1.92660.0512  0.6901 0.0639 B73 0.0108 0.0014 0.0032 0.0019 0.0132 0.00470.0261 0.0060  0^(c) — B51 5.4215 0.0307 2.5980 0.0525 7.4751 0.10806.8147 0.0943  6.9077 0.1968 B52 0.9658 0.0132 1.3712 0.0383 3.51210.0752 2.2447 0.0552  0.6960 0.0641 B5 unsplit 0.1565 0.0053 0.15220.0128 0.1288 0.0146 0.1546 0.0146  0.1307 0.0278 B5 total 6.5438 0.04354.1214 0.0747 11.1160 0.1504 9.2141 0.1324  7.7344 0.2784 B44 13.48380.0465 7.0137 0.0847 5.6807 0.0948 9.9253 0.1121 11.8024 0.2511 B450.5771 0.0102 4.8069 0.0708 0.1816 0.0173 1.8812 0.0506  0.7603 0.0670B12 unsplit 0.0788 0.0038 0.0280 0.0055 0.0049 0.0029 0.0193 0.0051 0.0654 0.0197 B12 total 14.1440 0.0474 11.8486 0.1072 5.8673 0.096311.8258 0.1210 12.6281 0.2584 B62 5.9117 0.0320 1.5267 0.0404 9.22490.1190 4.1825 0.0747  6.9421 0.1973 B63 0.4302 0.0088 1.8865 0.04480.4438 0.0270 0.8083 0.0333  0.3738 0.0471 B75 0.0104 0.0014 0.02260.0049 1.9673 0.0566 0.1101 0.0123  0.0356 0.0145 B76 0.0026 0.00070.0065 0.0026 0.0874 0.0120 0.0055 0.0028  0 — B77 0.0057 0.0010 0.01190.0036 0.0577 0.0098 0.0083 0.0034  0^(c) 0.0059 B15 unsplit 0.13050.0049 0.0691 0.0086 0.4301 0.0266 0.1820 0.0158  0.0059 0.0206 B15total 6.4910 0.0334 3.5232 0.0608 12.2112 0.1344 5.2967 0.0835  0.07150.2035  7.4290 B38 2.4413 0.0209 0.3323 0.0189 3.2818 0.0728 1.96520.0517  1.1017 0.0806 B39 1.9614 0.0188 1.2893 0.0371 2.0352 0.05766.3040 0.0909  4.5527 0.1615 B16 unsplit 0.0638 0.0034 0.0237 0.00510.0644 0.0103 0.1226 0.0130  0.0593 0.0188 B16 total 4.4667 0.02801.6453 0.0419 5.3814 0.0921 8.3917 0.1036  5.7137 0.1797 B57 3.59550.0252 5.6746 0.0766 2.5782 0.0647 2.1800 0.0544  2.7265 0.1260 B580.7152 0.0114 5.9546 0.0784 4.0189 0.0803 1.2481 0.0413  0.9398 0.0745B17 unsplit 0.2845 0.0072 0.3248 0.0187 0.3751 0.0248 0.1446 0.0141 0.2674 0.0398 B17 total 4.5952 0.0284 11.9540 0.1076 6.9722 0.10413.5727 0.0691  3.9338 0.1503 B49 1.6452 0.0172 2.6286 0.0528 0.24400.0200 2.3353 0.0562  1.5462 0.0953 B50 1.0580 0.0138 0.8636 0.03040.4421 0.0270 1.8883 0.0507  0.7862 0.0681 B21 unsplit 0.0702 0.00360.0270 0.0054 0.0132 0.0047 0.0771 0.0103  0.0356 0.0145 B21 total2.7733 0.0222 3.5192 0.0608 0.6993 0.0339 4.3007 0.0755  2.3680 0.1174B54 0.0124 0.0015 0.0183 0.0044 2.6873 0.0660 0.0289 0.0063  0.05340.0178 B55 1.9046 0.0185 0.4895 0.0229 2.2444 0.0604 0.9515 0.0361 1.4054 0.0909 B56 0.5527 0.0100 0.2686 0.0170 0.8260 0.0368 0.35960.0222  0.3387 0.0448 B22 unsplit 0.1682 0.0055 0.0496 0.0073 0.27300.0212 0.0372 0.0071  0.1246 0.0272 B22 total 2.0852 0.0217 0.82610.0297 6.0307 0.0971 1.3771 0.0433  1.9221 0.1060 B60 5.2222 0.03021.5299 0.0404 8.3254 0.1135 2.2538 0.0553  5.7218 0.1801 B61 1.19160.0147 0.4709 0.0225 6.2072 0.0989 4.6691 0.0788  2.6023 0.1231 B40unsplit 0.2696 0.0070 0.0388 0.0065 0.3205 0.0230 0.2473 0.0184  0.22710.0367 B40 total 6.6834 0.0338 2.0396 0.0465 14.8531 0.1462 7.17020.0963  8.5512 0.2168 BX 1.0922 0.0252 3.5258 0.0802 3.8749 0.09882.5266 0.0807  1.9867 0.1634

[0110] TABLE 3 Estimated gene frequencies of HLA-DR antigens CAU AFR ASILAT NAT Antigen Gf^(a) SE^(b) Gf SE Gf SE Gf SE Gf SE DR1 10.2279 0.04136.8200 0.0832 3.4628 0.0747 7.9859 0.1013 8.2512 0.2139 DR2 15.24080.0491 16.2373 0.1222 18.6162 0.1608 11.2389 0.1182 15.3932 0.2818 DR310.8708 0.0424 13.3080 0.1124 4.7223 0.0867 7.8998 0.1008 10.2549 0.2361DR4 16.7589 0.0511 5.7084 0.0765 15.4623 0.1490 20.5373 0.1520 19.82640.3123 DR6 14.3937 0.0479 18.6117 0.1291 13.4471 0.1404 17.0265 0.141114.8021 0.2772 DR7 13.2807 0.0463 10.1317 0.0997 6.9270 0.1040 10.67260.1155 10.4219 0.2378 DR8 2.8820 0.0227 6.2673 0.0800 6.5413 0.10139.7731 0.1110 6.0059 0.1844 DR9 1.0616 0.0139 2.9646 0.0559 9.75270.1218 1.0712 0.0383 2.8662 0.1291 DR10 1.4790 0.0163 2.0397 0.04652.2304 0.0602 1.8044 0.0495 1.0896 0.0801 DR11 9.3180 0.0396 10.61510.1018 4.7375 0.0869 7.0411 0.0955 5.3152 0.1740 DR12 1.9070 0.01854.1152 0.0655 10.1365 0.1239 1.7244 0.0484 2.0132 0.1086 DR5 unsplit1.2199 0.0149 2.2957 0.0493 1.4118 0.0480 1.8225 0.0498 1.6769 0.0992DR5 total 12.4449 0.0045 17.0260 0.1243 16.2858 0.1516 10.5880 0.11489.0052 0.2218 DRX 1.3598 0.0342 0.8853 0.0760 2.5521 0.1089 1.40230.0930 2.0834 0.2037

[0111] It has been observed that predicted epitopes often cluster at oneor more particular regions within the amino acid sequence of a TAA. Theidentification of such ECRs offers a simple and practicable solution tothe problem of designing effective vaccines for stimulating cellularimmunity. For vaccines in which immune epitopes are desired, an ECR isdirectly useful as a vaccine. This is because the immune proteasomes ofthe pAPCs can correctly process the cluster, liberating one or more ofthe contained MHC-binding peptides, in the same way a cell having immuneproteasomes activity processes and presents peptides derived from thecomplete TAA. The cluster is also a useful a starting material foridentification of housekeeping epitopes produced by the housekeepingproteasomes active in peripheral cells.

[0112] Identification of housekeeping epitopes using ECRs as a startingmaterial is described in copending U.S. patent application Ser. No.09/561,074 entitled “METHOD OF EPITOPE DISCOVERY,” filed Apr. 28, 2000,which is incorporated herein by reference in its entirety. Epitopesynchronization technology and vaccines for use in connection with thisinvention are disclosed in copending U.S. patent application Ser. No.09/560,465 entitled “EPITOPE SYNCHRONIZATION IN ANTIGEN PRESENTINGCELLS,” filed Apr. 28, 2000, which is incorporated herein by referencein its entirety. Nucleic acid constructs useful as vaccines inaccordance with the present invention are disclosed in copending U.S.patent application Ser. No. 09/561,572 entitled “EXPRESSION VECTORSENCODING EPITOPES OF TARGET-ASSOCIATED ANTIGENS,” filed Apr. 28, 2000,which is incorporated herein by reference in its entirety.

[0113] Vector Design and Vectors

[0114] Degradation of cytosolic proteins takes place via theubiquitin-dependent multi-catalytic multi-subunit protease system knownas the proteasome. The proteasome degrades cytosolic proteins generatingfragments that can then be translocated from the cytosol into theendoplasmic reticulum (ER) for loading onto class I MHC. Such proteinfragments shall be referred to as class I peptides. The peptide loadedMHC are subsequently transported to the cell surface where they can bedetected by CTL.

[0115] The multi-catalytic activity of the proteasome is the result ofits multi-subunit structure. Subunits are expressed from different genesand assembled post-translationally into the proteasome complex. A keyfeature of the proteasome is its bimodal activity, which enables it toexert its protease, or cleavage function, with two discrete kinds ofcleavage patterns. This bimodal action of the proteasome is extremelyfundamental to understanding how CTL are targeted to recognizeperipheral cells in the body and how this targeting requiressynchronization between the immune system and the targeted cells.

[0116] The housekeeping proteasome is constitutively active in allperipheral cells and tissues of the body. The first mode of operationfor the housekeeping proteasome is to degrade cellular protein,recycling it into amino acids. Proteasome function is therefore anecessary activity for cell life. As a corollary to its housekeepingprotease activity, however, class I peptides generated by thehousekeeping proteasome are presented on all of the peripheral cells ofthe body.

[0117] The proteasome's second mode of function is highly exclusive andoccurs specifically in pAPCs or as a consequence of a cellular responseto interferons (IFNs). In its second mode of activity the proteasomeincorporates unique subunits, which replace the catalytic subunits ofthe constitutive housekeeping proteasome. This “modified” proteasome hasbeen called the immunoproteasome, owing to its expression in pAPC and asa consequence of induction by IFN in body cells.

[0118] APC define the repertoire of CTL that recirculate through thebody and are potentially active as killer cells. CTL are activated byinteracting with class I peptide presented on the surface of a pAPC.Activated CTL are induced to proliferate and caused to recirculatethrough the body in search of diseased cells. This is why the CTLresponse in the body is defined specifically by the class I peptidesproduced by the pAPC. It is important to remember that pAPCs express theimmunoproteasome, and that as a consequence of the bimodal activity ofthe proteasome, the cleavage pattern of proteins (and the resultantclass I peptides produced) are different from those in peripheral bodycells which express housekeeping proteasome. The differential proteasomeactivity in pAPC and peripheral body cells, therefore, is important toconsider during natural infection and with therapeutic CTL vaccinationstrategies.

[0119] All cells of the body are capable of producing IFN in the eventthat they are infected by a pathogen such as a virus. IFN production inturn results in the expression of the immunoproteasome in the infectedcell. Viral antigens are thereby processed by the immunoproteasome ofthe infected cell and the consequent peptides are displayed with class IMHC on the cell surface. At the same time, pAPC are sequestering virusantigens and are processing class I peptides with their immunoproteasomeactivity, which is normal for the pAPC cell type. The CTL response inthe body is being stimulated specifically by the class I peptidesproduced by the pAPC. Fortunately, the infected cell is also producingclass I peptides from the immunoproteasome, rather than the normalhousekeeping proteasome. Thus, virus-related class I peptides are beingproduced that enable detection by the ensuing CTL response. The CTLimmune response is induced by pAPC, which normally produce differentclass I peptides compared to peripheral body cells, owing to differentproteasome activity. Therefore, during infection there is epitopesynchronization between the infected cell and the immune system.

[0120] This is not the case with tumors and chronic viruses, which blockthe interferon system. For tumors there is no infection in the tumorcell to induce the immunoproteasome expression, and chronic virusinfection either directly or indirectly blocks immunoproteasomeexpression. In both cases the diseased cell maintains its display ofclass I peptides derived from housekeeping proteasome activity andavoids effective surveillance by CTL.

[0121] In the case of therapeutic vaccination to eradicate tumors orchronic infections, the bimodal function of the proteasome and itsdifferential activity in APC and peripheral cells of the body issignificant. Upon vaccination with protein antigen, and before a CTLresponse can occur, the antigen must be acquired and processed intopeptides that are subsequently presented on class I MHC on the pAPCsurface. The activated CTL recirculate in search of cells with similarclass I peptide on the surface. Cells with this peptide will besubjected to destruction by the cytolytic activity of the CTL. If thetargeted diseased cell does not express the immunoproteasome, which ispresent in the pAPC, then the epitopes are not synchronized and CTL failto find the desired peptide target on the surface of the diseased cell.

[0122] Preferably, therapeutic vaccine design takes into account theclass I peptide that is actually present on the target tissue. That is,effective antigens used to stimulate CTL to attack diseased tissue arethose that are naturally processed and presented on the surface of thediseased tissue. For tumors and chronic infection this generally meansthat the CTL epitopes are those that have been processed by thehousekeeping proteasome. In order to generate an effective therapeuticvaccine, CTL epitopes are identified based on the knowledge that suchepitopes are, in fact, produced by the housekeeping proteasome system.Once identified, these epitopes, embodied as peptides, can be used tosuccessfully immunize or induce therapeutic CTL responses againsthousekeeping proteasome expressing target cells in the host.

[0123] However, in the case of DNA vaccines, there can be an additionalconsideration. The immunization with DNA requires that APCs take up theDNA and express the encoded proteins or peptides. It is possible toencode a discrete class I peptide on the DNA. By immunizing with thisconstruct, APCs can be caused to express a housekeeping epitope, whichis then displayed on class I MHC on the surface of the cell forstimulating an appropriate CTL response. Constructs for generation ofproper termini of housekeeping epitopes have been described in U.S.patent application Ser. No. 09/561,572 entitled EXPRESSION VECTORSENCODING EPITOPES OF TARGET-ASSOCIATED ANTIGENS, filed on Apr. 28, 2000,which is incorporated herein by reference in its entirety.

[0124] Embodiments of the invention provide expression cassettes thatencode one or more embedded housekeeping epitopes, and methods fordesigning and testing such expression cassettes. The expressioncassettes and constructs can encode epitopes, including housekeepingepitopes, derived from antigens that are associated with targets.Housekeeping epitopes can be liberated from the translation product(s)of the cassettes. For example, in some embodiments of the invention, thehousekeeping epitope(s) can be flanked by arbitrary sequences or bysequences incorporating residues known to be favored in immunoproteasomecleavage sites. In further embodiments of the invention multipleepitopes can be arrayed head-to-tail. In some embodiments, these arrayscan be made up entirely of housekeeping epitopes. Likewise, the arrayscan include alternating housekeeping and immune epitopes. Alternatively,the arrays can include housekeeping epitopes flanked by immune epitopes,whether complete or distally truncated. In some preferred embodiments,each housekeeping epitope can be flanked on either side by an immuneepitope, such that an array of such arrangements has two immune epitopesbetween each housekeeping epitope. Further, the arrays can be of anyother similar arrangement. There is no restriction on placing ahousekeeping epitope at the terminal positions of the array. The vectorscan additionally contain authentic protein coding sequences or segmentsthereof containing epitope clusters as a source of immune epitopes.

[0125] Several disclosures make reference to polyepitopes orstring-of-bead arrays. See, for example, WO0119408A1, Mar. 22, 2001;WO9955730A2, Nov. 4, 1999; WO0040261A2, Jul. 13, 2000; WO9603144A1, Feb.8, 1996; EP1181314A1, Feb. 27, 2002; WO0123577A3, April 5; U.S. Pat. No.6,074,817, Jun. 13, 2000; U.S. Pat. No. 5,965,381, Oct. 12, 1999;WO9741440A1, Nov. 6, 1997; U.S. Pat. No. 6,130,066, Oct. 10, 2000; U.S.Pat. No. 6,004,777, Dec. 21, 1999; U.S. Pat. No. 5,990,091, Nov. 23,1999; WO9840501A1, Sep. 17, 1998; WO9840500A1, Sep. 17, 1998;WO0118035A2, Mar. 15, 2001; WO02068654A2, Sep. 6, 2002; WO0189281A2,Nov. 29, 2001; WO0158478A, Aug. 16, 2001; EP1118860A1, Jul. 25, 2001;WO0111040A1, Feb. 15, 2001; WO0073438A1, Dec. 7, 2000; WO0071158A1, Nov.30, 2000; WO0066727A1, Nov. 9, 2000; WO0052451A1, Sep. 8, 2000;WO0052157A1, Sep. 8, 2000; WO0029008A2, May 25, 2000; WO0006723A1, Feb.10, 2000; all of which are incorporated by reference in their entirety.Additional disclosures, all of which are hereby incorporated byreference in their entirety, include Palmowski M J, et al—J Immunol2002;168(9):4391-8; Fang Z Y, et al—Virology 2001;291(2):272-84; FiratH, et al—J Gene Med 2002;4(1):38-45; Smith S G, et al—Clin Cancer Res2001;7(12):4253-61; Vonderheide R H, et al—Clin Cancer Res 2001;7(11):3343-8; Firat H, et al—Eur J Immunol 2001;31(10):3064-74; Le T T,et al—Vaccine 2001;19(32):4669-75; Fayolle C, et al—J Virol2001;75(16):7330-8; Smith S G—Curr Opin Mol Ther 1999;1(1):10-5; FiratH, et al—Eur J Immunol 1999;29(10):3112-21; Mateo L, et al—J Immunol1999;163(7):4058-63; Heemskerk M H, et al—Cell Immunol 1999;195(1):10-7;Woodberry T, et al—J Virol 1999;73(7):5320-5; Hanke T, et al—Vaccine1998;16(4):426-35; Thomson S A, et al—J Immunol 1998;160(4):1717-23;Toes R E, et al—Proc Natl Acad Sci USA 1997;94(26):14660-5; Thomson S A,et al—J Immunol 1996;157(2):822-6; Thomson S A, et al—Proc Natl Acad SciUSA 1995;92(13):5845-9; Street M D, et al—Immunology 2002;106(4):526-36;Hirano K, et al—Histochem Cell Biol 2002;117(1):41-53; Ward S M, etal—Virus Genes 2001;23(1):97-104; Liu W J, et al—Virology2000;273(2):374-82; Gariglio P, et al—Arch Med Res 1998;29(4):279-84;Suhrbier A—Immunol Cell Biol 1997;75(4):402-8; Fomsgaard A, etal—Vaccine 1999;18(7-8):681-91; An L L, et al—J Virol1997;71(3):2292-302; Whitton J L, et al—J Virol 1993;67(1):348-52;Ripalti A, et al—J Clin Microbiol 1994;32(2):358-63; and Gilbert, S. C.,et al., Nat. Biotech. 15:1280-1284, 1997.

[0126] One important feature that the disclosures in the precedingparagraph all share is their lack of appreciation for the desirabilityof regenerating housekeeping epitopes when the construct is expressed ina pAPC. This understanding was not apparent until the present invention.Embodiments of the invention include sequences, that when processed byan immune proteasome, liberate or generate a housekeeping epitope.Embodiments of the invention also can liberate or generate such epitopesin immunogenically effective amounts. Accordingly, while the precedingreferences contain disclosures relating to polyepitope arrays, none isenabling of the technology necessary to provide or select a polyepitopecapable of liberating a housekeeping epitope by action of animmunoproteasome in a pAPC. In contrast, embodiments of the instantinvention are based upon a recognition of the desirability of achievingthis result. Accordingly, embodiments of the instant invention includeany nucleic acid construct that encodes a polypeptide containing atleast one housekeeping epitope provided in a context that promotes itsgeneration via immunoproteasomal activity, whether the housekeepingepitope is embedded in a string-of-beads array or some otherarrangement. Some embodiments of the invention include uses of one ormore of the nucleic acid constructs or their products that arespecifically disclosed in any one or more of the above-listedreferences. Such uses include, for example, screening a polyepitope forproper liberation context of a housekeeping epitope and/or an immuneepitope, designing an effective immunogen capable of causingpresentation of a housekeeping epitope and/or an immune epitope on apAPC, immunizing a patient, and the like. Alternative embodimentsinclude use of only a subset of such nucleic acid constructs or a singlesuch construct, while specifically excluding one or more other suchconstructs, for any of the purposes disclosed herein. Some preferredembodiments employ these and/or other nucleic acid sequences encodingpolyepitope arrays alone or in combination. For example, someembodiments exclude use of polyepitope arrays from one or more of theabove-mentioned references. Other embodiments may exclude anycombination or all of the polyepitope arrays from the above-mentionedreferences collectively. Some embodiments include viral and/or bacterialvectors encoding polyepitope arrays, while other embodimentsspecifically exclude such vectors. Such vectors can encode carrierproteins that may have some immunostimulatory effect. Some embodimentsinclude such vectors with such immunostimulatory/immunopotentiatingeffects, as opposed to immunogenic effects, while in other embodimentssuch vectors may be included. Further, in some instances viral andbacterial vectors encode the desired epitope as a part of substantiallycomplete proteins which are not associated with the target cell. Suchvectors and products are included in some embodiments, while excludedfrom others. Some embodiments relate to repeated administration ofvectors. In some of those embodiments, nonviral and nonbacterial vectorsare included. Likewise, some embodiments include arrays that containextra amino acids between epitopes, for example anywhere from 1-6 aminoacids, or more, in some embodiments, while other embodimentsspecifically exclude such arrays.

[0127] Embodiments of the present invention also include methods, uses,therapies, and compositions directed to various types of targets. Suchtargets can include, for example, neoplastic cells such as those listedbelow, for example; and cells infected with any virus, bacterium,protozoan, fungus, or other agents, examples of which are listed below,in Tables 4-8, or which are disclosed in any of the references listedabove. Alternative embodiments include the use of only a subset of suchneoplastic cells and infected cells listed below, in Tables 4-8, or inany of the references disclosed herein, or a single one of theneoplastic cells or infected cells, while specifically excluding one ormore other such neoplastic cells or infected cells, for any of thepurposes disclosed herein. The following are examples of neoplasticcells that can be targeted: human sarcomas and carcinomas, e.g.,fibrosarcoma, myxosarcoma, liposarcoma, chondrosarcoma, osteogenicsarcoma, chordoma, angiosarcoma, endotheliosarcoma, lymphangiosarcoma,lymphangioendotheliosarcoma, synovioma, mesothelioma, Ewing's tumor,leiomyosarcoma, rhabdomyosarcoma, colon carcinoma, pancreatic cancer,breast cancer, ovarian cancer, prostate cancer, squamous cell carcinoma,basal cell carcinoma, adenocarcinoma, sweat gland carcinoma, sebaceousgland carcinoma, papillary carcinoma, papillary adenocarcinomas,cystadenocarcinoma, medullary carcinoma, bronchogenic carcinoma, renalcell carcinoma, hepatoma, bile duct carcinoma, choriocarcinoma,seminoma, embryonal carcinoma, Wilms' tumor, cervical cancer, testiculartumor, lung carcinoma, small cell lung carcinoma, bladder carcinoma,epithelial carcinoma, glioma, astrocytoma, medulloblastoma,craniopharyngioma, ependymoma, pinealoma, hemangioblastoma, acousticneuroma, oligodendroglioma, meningioma, melanoma, neuroblastoma,retinoblastoma; leukemias, e.g., acute lymphocytic leukemia and acutemyelocytic leukemia (myeloblastic, promyelocytic, myelomonocytic,monocytic and erythroleukemia); chronic leukemia (chronic myelocytic(granulocytic) leukemia and chronic lymphocytic leukemia); andpolycythemia vera, lymphoma (Hodgkin's disease and non Hodgkin'sdisease), multiple myeloma, Waldenstrom's macroglobulinemia, heavy chaindisease, hepatocellular cancer, brain cancer, stomach cancer, livercancer, and the like. Examples of infectious agents that infect thetarget cells can include the following: adenovirus, cytomegalovirus,Epstein-Barr virus, herpes simplex virus 1, herpes simplex virus 2,human herpesvirus 6, varicella-zoster virus, hepatitis B virus,hepatitis D virus, papilloma virus, parvovirus B19, polyomavirus BK,polyomavirus JC, hepatitis C virus, measles virus, rubella virus, humanimmunodeficiency virus (HIV), human T cell leukemia virus I, human Tcell leukemia virus II, Chlamydia, Listeria, Salmonella, Legionella,Brucella, Coxiella, Rickettsia, Mycobacterium, Leishmania, Trypanasoma,Toxoplasma, Plasmodium, and the like. Exemplary infectious agents andneoplastic cells are also included in Tables 4-8 below.

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[0129] Additional embodiments of the invention include methods, uses,therapies, and compositions relating to a particular antigen, whetherthe antigen is derived from, for example, a target cell or an infectiveagent, such as those mentioned above. Some preferred embodiments employthe antigens listed herein, in Tables 4-8, or in the list below, alone,as subsets, or in any combination. For example, some embodiments excludeuse of one or more of those antigens. Other embodiments may exclude anycombination or all of those antigens. Several examples of such antigensinclude MelanA (MART-1), gp100 (Pmel 17), tyrosinase, TRP-1, TRP-2,MAGE-1, MAGE-3, BAGE, GAGE-1, GAGE-2, CEA, RAGE, NY-ESO, SCP-1,Hom/Mel-40, PRAME, p53, H-Ras, HER-2/neu, BCR-ABL, E2A-PRL, H4-RET,IGH-IGK, MYL-RAR, Epstein Barr virus antigens, EBNA, humanpapillomavirus (HPV) antigens E6 and E7, TSP-180, MAGE-4, MAGE-5,MAGE-6, p185erbB2, p180erbB-3, c-met, nm-23H1, PSA, TAG-72-4, CAM 17.1,NuMa, K-ras, β-Catenin, CDK4, Mum-1, p16, as well as any of those setforth in the above mentioned references. Other antigens are included inTables 4-7 below.

[0130] Further embodiments include methods, uses, compositions, andtherapies relating to epitopes, including, for example those epitopeslisted in Tables 4-8. These epitopes can be useful to flank housekeepingepitopes in screening vectors, for example. Some embodiments include oneor more epitopes from Tables 4-8, while other embodiments specificallyexclude one or more of such epitopes or combinations thereof. TABLE 4 AAT cell epitope MHC Virus Protein Position ligand (Antigen) MHC moleculeAdenovirus 3 E3 9Kd 30-38 LIVIGILIL HLA-A*0201 (SEQ. ID NO.:44)Adenovirus 5 EIA 234-243 SGPSNTPPEI H2-Db (SEQ. ID NO.:45) Adenovirus 5EIB 192-200 VNIRNCCYI H2-Db (SEQ. ID NO.:46) Adenovirus 5 EIA 234-243SGPSNIPPEI (T>I) H2-Db (SEQ. ID NO.:47) CSFV NS 2276-2284 ENALLVALF SLA,haplotype polyprotein (SEQ. ID NO.:48) d/d Dengue virus 4 NS3 500-508TPEGIIPTL HLA-B*3501 (SEQ. ID NO.:49) EBV LMIP-2 426-434 CLGGLLTMVHLA-A*0201 (SEQ. ID NO.:50) EBV EBNA-1 480-484 NIAEGLRAL HLA-A*0201(SEQ. ID NO.:51) EBV EBNA-1 519-527 NLRRGTALA HLA-A*0201 (SEQ. IDNO.:52) EBV EBNA-1 525-533 ALAIPQCRL HLA-A*0201 (SEQ. ID NO.:53) EBVEBNA-1 575-582 VLKDAIKDL HLA-A*0201 (SEQ. ID NO.:54) EBV EBNA-1 562-570FMVFLQTHI HLA-A*0201 (SEQ. ID NO.:55) EBV EBNA-2 15-23 HLIVDTDSLHLA-A*0201 (SEQ. ID NO.:56) EBV EBNA-2 22-30 SLGNPSLSV HLA-A*0201 (SEQ.ID NO.:57) EBV EBNA-2 126-134 PLASAMRML HLA-A*0201 (SEQ. ID NO.:58) EBVEBNA-2 132-140 RMLWMANYI HL.A-A*0201 (SEQ. ID NO.:59) EBV EBNA-2 133-141MLWMANYIV HLA-A*0201 SEQ. ID NO.:60) EBV EBNA-2 151-159 ILPQGPQTAHLA-A*0201 (SEQ. ID NO.:61) EBV EBNA-2 171-179 PLRPTAPTI HLA-A*0201(SEQ. ID NO.:62) EBV EBNA-2 205-213 PLPPATLTV HLA-A*0201 (SEQ. IDNO.:63) EBV EBNA-2 246-254 RMHLPVLHV HLA-A*0201 (SEQ. ID NO.:64) EBVEBNA-2 287-295 PMPLPPSQL HLA-A*0201 (SEQ. ID NO.:65) EBV EBNA-2 294-302QLPPPAAPA HLA-A*0201 (SEQ. ID NO.:66) EBV EBNA-2 381-389 SMPELSPVLHLA-A*0201 (SEQ. ID NO.:67) EBV EBNA-2 453-461 DLDESWDYI HLA-A*0201(SEQ. ID NO.:68) EBV BZLF1 43-51 PLPCVLWPV HLA-A*0201 (SEQ. ID NO.:69)EBV BZLF1 167-175 SLEECDSEL HLA-A*0201 (SEQ. ID NO.:70) EBV BZLF1176-184 EIKRYKNRV HLA-A*0201 (SEQ. ID NO.:71) EBV BZLF1 195-203QLLQHYREV HLA-A*0201 (SEQ. ID NO.:72) EBV BZLF1 196-204 LLQHYREVAHLA-A*0201 (SEQ. ID NO.:73) EBV BZLFI 217-225 LLKQMCPSL HLA-A*0201 (SEQ.ID NO.:74) EBV BZLF1 229-237 SIIPRTPDV HLA-A*0201 (SEQ. ID NO.:75) EBVEBNA-6 284-293 LLDFVRFMGV HLA-A*0201 (SEQ. ID NO.:76) EBV EBNA-3 464-472SVRDRLARL HLA-A*0203 (SEQ. ID NO.:77) EBV EBNA-4 416-424 IVTDFSVIKHLA-A*1101 (SEQ. ID NO.:78) EBV EBNA-4 399-408 AVFDRKSDAK HLA-A*0201(SEQ. ID NO.:79) EBV EBNA-3 246-253 RYSIFFDY HLA-A24 (SEQ. ID NO.:80)EBV EBNA-6 881-889 QPRAPIRPI HLA-B7 (SEQ. ID NO.:81) EBV EBNA-3 379-387RPPIFIRRI. HLA-B7 (SEQ. ID NO.:82) EBV EBNA-1 426-434 EPDVPPGAI HLA-B7(SEQ. ID NO.:83) EBV EBNA-1 228-236 IPQCRLTPL HLA-B7 (SEQ. ID NO.:84)EBV EBNA-1 546-554 GPGPQPGPL HLA-B7 (SEQ. ID NO.:85) EBV EBNA-1 550-558QPGPLRESI HLA-B7 (SEQ. ID NO.:86) EBV EBNA-1 72-80 R.PQKRPSCI HLA-B7(SEQ. ID NO.:87) EBV EBNA-2 224-232 PPTPLLTVL HLA-B7 (SEQ. ID NO.:88)EBV EBNA-2 241-249 TPSPPRMHL HLA-B7 (SEQ. ID NO.:89) EBV EBNA-2 244-252PPRMHLPVL HLA-B7 (SEQ. ID NO.:90) EBV EBNA-2 254-262 VPDQSMHPL HLA-B7(SEQ. ID NO.:91) EBV EBNA-2 446-454 PPSIDPADL HLA-B7 (SEQ. ID NO.:92)EBV BZLFI 44-52 LPCVLWPVL HLA-B7 (SEQ. ID NO.:93) EBV BZLF1 222-231CPSLDVDSII HLA-B7 (SEQ. ID NO.:94) EBV BZLFI 234-242 TPDVLHEDL HLA-B7(SEQ. ID NO.:95) EBV EBNA-3 339-347 FLRGRAYGL HLA-B8 (SEQ. ID NO.:96)EBV EBNA-3 26-34 QAKWRLQTL HLA-B8 (SEQ. ID NO.:97) EBV EBNA-3 325-333AYPLHEQHG HLA-B8 (SEQ. ID NO.:98) EBV EBNA-3 158-166 YIKSFVSDA HLA-B8(SEQ. ID NO.:99) EBV LMP-2 236-244 RRRWRRLTV HLA-B*2704 (SEQ. IDNO.:100) EBV EBNA-6 258-266 RRIYDLIEL HLA-B*2705 (SEQ. ID NO.:101) EBVEBNA-3 458-466 YPLHEQHGM HLA-B*3501 (SEQ. ID NO.:102) EBV EBNA-3 458-466YPLHEQHGM HLA-B*3503 (SEQ. ID NO.:103) HCV NS3 389-397 HSKKKCDEL HLA-B8(SEQ. ID NO.:104) HCV env E 44-51 ASRCWVAM HLA-B*3501 (SEQ. ID NO.:105)HCV core 27-35 GQIVGGVYL HLA-B*40012 protein (SEQ. ID NO.:106) HCV NSI77-85 PPLTDFDQGW HLA-B*5301 (SEQ. ID NO.:107) HCV core 18-27 LMGYIPLVGAH2-Dd protein (SEQ. ID NO.:108) HCV core 16-25 ADLMGYIPLV H2-Dd protein(SEQ. ID NO.:109) HCV NS5 409-424 MSYSWTGALVTPCAEE H2-Dd (SEQ. IDNO.:110) HCV NS1 205-213 KHPDATYSR Papa-A06 (SEQ. ID NO.:111) HCV-1 NS3400-409 KLVALGINAV HLA-A*0201 (SEQ. ID NO.:112) HCV-1 NS3 440-448GDFDSVIDC Patr-B16 (SEQ. ID NO.:113) HCV-1 env E 118-126 GNASRCWVAPatr-B16 (SEQ. ID NO.:114) HCV-1 NS1 159-167 TRPPLGNWF Patr-B13 (SEQ. IDNO.:115) HCV-1 NS3 351-359 VPHPNIEEV Patr-B13 (SEQ. ID NO.:116) HCV-1NS3 438-446 YTGDFDSVI Patr-B01 (SEQ. ID NO.:117) HCV-1 NS4 328-335SWAIKWEY Patr-Al 1 (SEQ. ID NO.:118) HCV-1 NSI 205-213 KHPDATYSRPatr-A04 (SEQ. ID NO.:119) HCV-1 NS3 440-448 GDFDSVIDC Patr-A04 (SEQ. IDNO.:120) HIV gp41 583-591 RYLKDQQLL HLA A24 (SEQ. ID NO.:121) HIV gagp24267-275 IVGLNKIVR HLA-A*3302 (SEQ. ID NO.:122) HIV gagp24 262-270EIYKRWIIL HLA-B8 (SEQ. ID NO.:123) HIV gagp24 261-269 GElYKRWI1 HLA-B8(SEQ. ID NO.:124) HIV gagp17 93-101 EIKDTKEAL HLA-B8 (SEQ. ID NO.:125)HTV gp41 586-593 YLKDQQLL HLA-B8 (SEQ. ID NO.:126) HIV gagp24 267-277ILGLNKIVRMY HLA-B* 1501 (SEQ. ID NO.:127) HIV gp41 584-592 ERYLKDQQLHLA-B14 (SEQ. ID NO.:128) HIV nef 115-125 YHTQGYFPQWQ HLA-B17 (SEQ. IDNO.:129) HIV nef 117-128 TQGYFPQWQNYT HLA-B17 (SEQ. ID NO.:130) HIVgp120 314-322 GRAFVTIGK HLA-B*2705 (SEQ. ID NO.:131) HIV gagp24 263-271KRWIILGLN HLA-B*2702 (SEQ. ID NO.:132) HIV nef 72-82 QVPLRPMTYKHLA-B*3501 (SEQ. ID NO.:133) HIV nef 117-125 TQGYFPQWQ HLA-B*3701 (SEQ.ID NO.:134) HIV gagp24 143-151 HQAISPRTI, HLA-Cw*0301 (SEQ. ID NO.:135)HIV gagp24 140-151 QMVHQAISPRTL HLA-Cw*0301 (SEQ. ID NO.:136) HIV gp120431-440 MYAPPIGGQI H2-Kd (SEQ. ID NO.:137) HIV gp160 318-327 RGPGRAFVTIH2-Dd (SEQ. ID NO.:138) HIV gp120 17-29 MPGRAFVTI H2-Ld (SEQ. IDNO.:139) HIV-1 RT 476-484 ILKEPVHGV HLA-A*0201 (SEQ. ID NO.:140) HIV-1nef 190-198 AFHHVAREL HLA-A*0201 (SEQ. ID NO.:141) HIV-1 gpI60 120-128KLTPLCVTL HLA-A*0201 (SEQ. ID NO.:142) HIV-1 gp]60 814-823 SLLNATDIAVHLA-A*0201 (SEQ. ID NO.:143) HIV-1 RT 179-187 VIYQYMDDL HLA-A*0201 (SEQ.ID NO.:144) HIV-1 gagp 17 77-85 SLYNTVATL HLA-A*0201 (SEQ. ID NO.:145)HIV-1 gp160 315-329 RGPGRAFVT1 HLA-A*0201 (SEQ. ID NO.:146) HIV-1 gp41768-778 RLRDLLLIVTR HLA-A3 (SEQ. ID NO.:147) HIV-1 nef 73-82 QVPLRPMTYKHLA-A3 (SEQ. ID NO.:148) HIV-1 gp120 36-45 TVYYGVPVWK HLA-A3 (SEQ. IDNO.:149) HIV-1 gagp17 20-29 RLRPGGKKK HLA-A3 (SEQ. ID NO.:150) HIV-1gp120 38-46 VYYGVPVWK HLA-A3 (SEQ. ID NO.:151) HIV-1 nef 74-82 VPLRPMTYKHLA-a*1101 (SEQ. ID NO.:152) HIV-1 gagp24 325-333 AIFQSSMTK HLA-A*1101(SEQ. ID NO.:153) HIV-1 nef 73-82 QVPLRPMTYK HLA-A*1101 (SEQ. IDNO.:154) HIV-1 nef 83-94 AAVDLSHFLKEK HLA-A*1101 (SEQ. ID NO.:155) HIV-1gagp24 349-359 ACQGVGGPGGHK HLA-A*1101 (SEQ. 110 NO.:156) HIV-1 gagp24203-212 ETINEEAAEW HLA-A25 (SEQ. ID NO.:157) HIV-1 nef 128-137TPGPGVRYPL HLA-B7 (SEQ. ID NO.:158) HIV-1 gagp 17 24-31 GGKKKYKL HLA-B8(SEQ. ID NO.:159) HIV-1 gp120  2-10 RVKEKYQHL HLA-B8 (SEQ. ID NO.:160)HIV-1 gagp24 298-306 DRFYKTLRA HLA-B 14 (SEQ. ID NO.:161) HIV-1 NEF132-147 GVRYPLTFGWCYKLVP HLA-B18 (SEQ. ID NO.:162) HIV-1 gagp24 265-24KRWIILGLNK HLA-B*2705 (SEQ. ID NO.:163) HIV-1 nef 190-198 AFHHVARELHLA-B*5201 (SEQ. ID NO.:164) EBV EBNA-6 335-343 KEHVIQNAF HLA-B44 (SEQ.ID NO.:165) EBV EBNA-6 130-139 EENLLDFVRF HLA-B*4403 (SEQ. ID NO.:166)EBV EBNA-2 42-51 DTPLIPLTIF HLA-B51 (SEQ. ID NO.:167) EBV EBNA-6 213-222QNGALAINTF HLA-1362 (SEQ. ID NO.:168) EBV EBNA-3 603-611 RLRAEAGVKHLA-A3 (SEQ. ID NO.:169) HBV sAg 348-357 GLSPTVWLSV HLA-A*0201 (SEQ. IDNO.:170) HBV SAg 335-343 WLSLLVPFV HLA-A*0201 (SEQ. ID NO.:171) HBV cAg18-27 FLPSDFFPSV HLA-A*0201 (SEQ. ID NO.:172) HBV cAg 18-27 FLPSDFFPSVHLA-A*0202 (SEQ. ID NO.:173) HBV cAg 18-27 FLPSDFFPSV HLA-A*0205 (SEQ.ID NO.:174) HBV cAg 18-27 FLPSDFFPSV HLA-A*0206 (SEQ. ID NO.:175) HBVpol 575-583 FLLSLGIHL HLA-A*0201 (SEQ. ID NO.:176) HBV pol 816-824SLYADSPSV HLA-A*0201 (SEQ. ID NO.:177) HBV pol 455-463 GLSRYVARLHLA-A*0201 (SEQ. ID NO.:178) HBV env 338-347 LLVPFVQWFV HLA-A*0201 (SEQ.ID NO.:179) HBV pol 642-650 ALMPLYACI HLA-A*0201 (SEQ. ID NO.:180) HBVenv 378-387 LLPIFFCLWV HLA-A*0201 (SEQ. ID NO.:181) HEy pol 538-546YMDDVVLGA HLA-A*0201 (SEQ. ID NO.:182) HBV env 250-258 LLLCLIFLLHLA-A*0201 (SEQ. ID NO.:183) HBV env 260-269 LLDYQGMLPV HLA-A*0201 (SEQ.ID NO.:184) HBV env 370-379 SIVSPFIPLL HLA-A*0201 (SEQ. ID NO.:185) HBVenv 183-191 FLLTRILTI HLA-A*0201 (SEQ. ID NO.:186) HBV cAg 88-96YVNVNMGLK HLA-A* 1101 (SEQ. ID NO.:187) HBV cAg 141-151 STLPETTVVRRHLA-A*3101 (SEQ. ID NO.:188) HBV cAg 141-151 STLPETTVVRR HLA-A*6801(SEQ. ID NO.:189) HBV cAg 18-27 FLPSDFFPSV HLA-A*6801 (SEQ. ID NO.:190)HBV cAg 28-39 IPQSLDSWWTSL H2-Ld (SEQ. ID NO.:191) HBV cAg  93-100MGLKFRQL H2-Kb (SEQ. ID NO.:192) HBV preS 141-149 STBXQSGXQ HLA-A*0201(SEQ. ID NO.:193) HCMV gp B 618-628 FIAGNSAYEYV HLA-A*0201 (SEQ. lIDNO.:194) HCMV E1 978-989 SDEEFAIVAYTL HLA-B18 (SEQ. ID NO.:195) HCMVpp65 397-411 DDVWTSGSDSDEELV HLA-b35 (SEQ. ID NO.:196) HCMV pp65 123-131IPSINVHHY HLA-B*3501 (SEQ. ID NO.:197) HCMV pp65 495-504 NLVPMVATVOHLA-A*0201 (SEQ. ID NO.:198) HCMV pp65 415-429 RKTPRVTOGGAMAGA HLA-B7(SEQ. lID NO.:199) HCV MP 17-25 DLMGYIPLV HLA-A*0201 (SEQ. ID NO.:200)HCV MP 63-72 LLALLSCLTV HLA-A*0201 (SEQ. ID NO.:201) HCV MP 105-112ILHTPGCV HLA-A*0201 (SEQ. ID NO.:202) HCV env E 66-75 QLRRHIDLLVHLA-A*0201 (SEQ. ID NO.:203) HCV env E 88-96 DLCGSVFLV HLA-A*0201 (SEQ.ID NO.:204) HCV env E 172-180 SMVGNWAKV HLA-A*0201 (SEQ. ID NO.:205) HCVNSI 308-316 HLIIQNIVDV HLA-A*0201 (SEQ. ID NO.:206) HCV NSI 340-348FLLLADARV HLA-A*0201 (SEQ. ID NO.:207) (SEQ. liD NO.:208) HCV NSI 18-28SLLAPGAKQNV HLA-A*0201 (SEQ. ID NO.:209) HCV NSI 19-28 LLAPGAKQNVHLA-A*0201 (SEQ. ID NO.:210) HCV NS4 192-201 LLFNILGGWV HLA-A*0201 (SEQ.ID NO.:211) HCV NS3 579-587 YLVAYQATV HLA-A*0201 (SEQ. ID NO.:212) HCVcore 34-43 YLLPRRGPRL HLA-A*0201 protein (SEQ. ID NO.:213) HCV MP 63-72LLALLSCLTI HLA-A*0201 (SEQ. ID NO.:214) HCV NS4 174-182 SLMAFTAAVHLA-A*0201 (SEQ. ID NO.:215) HCV NS3 67-75 CINGVCTV HLA-A*0201 (SEQ. IDNO.:216) HCV NS3 163-171 LLCPAGHAV HLA-A*0201 (SEQ. ID NO.:217) HCV NS5239-247 ILDSFDPLV HLA-A*0201 (SEQ. ID NO.:218) HCV NS4A 236-244ILAGYGAGV HLA-A*0201 (SEQ. ID NO.:219) HCV NS5 714-722 GLQDCTMLVHLA-A*0201 (SEQ. ID NO.:220) HCV NS3 281-290 TGAPVTYSTY HLA-A*0201 (SEQ.ID NO.:221) HCV NS4A 149-157 HMWNFISGI HLA-A*0201 (SEQ. ID NO.:222) HCVNS5 575-583 RVCEKMALY HLA-A*0201-A3 (SEQ. ID NO.:223) HCV NS1 238-246TINYTIFK HLA-A*1101 (SEQ. ID NO.:224) HCV NS2 109-116 YISWCLWW HLA-A23(SEQ. ID NO.:225) HCV core 40-48 GPRLGVRAT HLA-B7 protein (SEQ. IDNO.:226) HIV-1 gp120 380-388 SFNCGGEFF HLA-Cw*0401 (SEQ. ID NO.:227)HIV-1 RT 206-214 TEMEKEGKI H2-Kk (SEQ. ID NO.:228) HIV-1 p17 18-26KIRLRPGGK HLA-A*0301 (SEQ. ID NO.:229) HIV-1 P17 20-29 RLRPGGKKKYHLA-A*0301 (SEQ. ID NO.:230) HIV-I RT 325-333 AIFQSSMTK HLA-A*0301 (SEQ.ID NO.:231) HIV-1 p17 84-92 TLYCVHQRI HLA-A11 (SEQ. ID NO.:232) HIV-1 RT508-517 IYQEPFKNLK HLA-A11 (SEQ. ID NO.:233) HIV-1 p17 28-36 KYKLKHIVWHLA-A24 (SEQ. ID NO.:234) HIV-1 gp120 53-62 LFCASDAKAY HLA-A24 (SEQ. IDNO.:235) HIV-1 gagp24 145-155 QAISPRTLNAW HLA-A25 (SEQ. ID NO.:236)HIV-1 gagp24 167-175 EVIPMFSAL HLA-A26 (SEQ. ID NO.:237) HIV-1 RT593-603 ETFYVDGAANR HLA-A26 (SEQ. ID NO.:238) HIV-1 gp41 775-785RLRDLLLIVTR HLA-A31 (SEQ. ID NO.:239) HIV-1 RT 559-568 PIQKETWETWHLA-A32 (SEQ. ID NO.:240) HIV-1 gp120 419-427 RIKQIINMW HLA-A32 (SEQ. IDNO.:241) HIV-1 RT 71-79 ITLWQRPLV HLA-A*6802 (SEQ. ID NO.:242) HIV-1 RT85-93 DTVLEEMNL HLA-A*6802 (SEQ. ID NO.:243) HIV-1 RT 71-79 ITLWQRPLVHLA-A*7401 (SEQ. ID NO.:244) HIV-1 gagp24 148-156 SPRTLNAWV HLA-B7 (SEQ.ID NO.:245) HIV-1 gagp24 179-187 ATPQDLNTM HLA-B7 (SEQ. ID NO.:246)HIV-1 gp120 303-312 RPNNNTRKSI HLA-B7 (SEQ. ID NO.:247) HIV-1 gp41843-851 IPRRIRQGL HLA-B7 (SEQ. ID NO.:248) HIV-1 p17 74-82 ELRSLYNTVHLA-B8 (SEQ. ID NO.:249) HIV-1 nef 13-20 WPTVRERM HLA-B8 (SEQ. IDNO.:250) HIV-1 nef 90-97 FLKEKGGL HLA-B8 (SEQ. ID NO.:251) HIV-1 gagp24183-191 DLNTMLNTV HLA-B14 (SEQ. iD NO.:252) HIV-1 P17 18-27 KIRLRPGGKKHLA-B27 (SEQ. ID NO.:253) HIV-1 p17 19-27 IRLRPGGKK HLA-B27 (SEQ. IDNO.:254) HIV-1 gp41 791-799 GRRGWEALKY HLA-B27 (SEQ. ID NO.:255) HIV-1nef 73-82 QVPLRPMTYK HLA-B27 (SEQ. ID NO.:256) HIV-1 GP41 590-597RYLKDQQL 11LA-B27 (SEQ. ID NO.:257) HIV-1 nef 105-114 RRQDILDLWIHLA-B*2705 (SEQ. ID NO.:258) HIV-1 nef 134-141 RYPLTFGW HLA-B*2705 (SEQ.ID NO.:259) HIV-1 p17 36-44 WASRELERF HLA-B35 (SEQ. ID NO.:260) HIV-1GAGP24 262-270 TVLDVGDAY HLA-B35 (SEQ. ID NO.:261) HIV-1 gp120 42-52VPVWKEATTTL HLA-B35 (SEQ. ID NO.:262) HIV-1 P17 36-44 NSSKVSQNY HLA-B35(SEQ. ID NO.:263) HIV-1 gagp24 254-262 PPIPVGDIY HLA-B35 (SEQ. IDNO.:264) HIV-1 RT 342-350 HPDIVIYQY HLA-B35 (SEQ. ID NO.:265) HIV-1 gp41611-619 TAVPWNASW HLA-B35 (SEQ. ID NO.:266) HIV-1 gag 245-253 NPVPVGNIYHLA-B35 (SEQ. ID NO.:267) HIV-1 nef 120-128 YFPDWQNYT HLA-B37 (SEQ. IDNO.:268) HIV-1 gagp24 193-201 GHQAAMQML HLA-B42 (SEQ. ID NO.:269) HIV-1p17 20-29 RLRPGGKKKY HLA-B42 (SEQ. ID NO.:270) HIV-1 RT 438-446YPGIKVRQL HLA-B42 (SEQ. ID NO.:271) HIV-1 RT 591-600 GAETFYVDGA HLA-B45(SEQ. ID NO.:272) HIV-1 gagp24 325-333 NANPDCKTI HLA-B51 (SEQ. IDNO.:273) HIV-1 gagp24 275-282 RMYSPTSI HLA-B52 (SEQ. ID NO.:274) HLV-1gp120 42-51 VPVWKEATTT HLA-B*5501 (SEQ. iD NO.:275) HIV-1 gagp24 147-155ISPRTLNAW HLA-B57 (SEQ. ID NO.:276) HIV-1 gagp24 240-249 TSTLQEQIGWHLA-B57 (SEQ. ID NO.:277) HIV-1 gagp24 162-172 KAFSPEVIPMF HLA-B57 (SEQ.ID NO.:278) HIV-1 gagp24 311-319 QASQEVKNW HLA-B57 (SEQ. ID NO.:279)HIV-1 gagp24 311-319 QASQDVKNW HLA-B57 (SEQ. ID NO.:280) HIV-1 nef116-125 HTQGYFPDWQ HLA-B57 (SEQ. ID NO.:281) HIV-1 nef 120-128 YFPDWQNYTHLA-B57 (SEQ. ID NO.:282) HIV-1 gagp24 240-249 TSTLQEQIGW HLA-B58 (SEQ.ID NO.:283) HIV-1 p17 20-29 RLRPGGKKKY HLA-B62 (SEQ. ID NO.:284) HIV-1P24 268-277 LGLNKJVRMY HLA-B62 (SEQ. ID NO.:285) HIV-1 RT 415-426LVGKLNWASQIY HLA-B62 (SEQ. ID NO.:286) HIV-1 RT 476-485 ILKEPVHGVYHLA-B62 (SEQ. ID NO.:287) HIV-1 nef 117-127 TQGYFPDWQNY HLA-B62 (SEQ. IDNO.:288) HIV-1 nef 84-91 AVDLSHFL HLA-B62 (SEQ. ID NO.:289) HIV-1 gagp24168-175 VIPMFSAL HLA-Cw*0102 (SEQ. ID NO.:290) HLV-1 p120 376-384FNCGGEFFY HLA-A29 (SEQ. ID NO.:291) HIV-1 gp120 375-383 SFNCGGEFFHLA-B15 (SEQ. ID NO.:292) HIV-1 nef 136-145 PLTFGWCYKL HLA-A*0201 (SEQ.ID NO.:293) HIV-1 nef 180-189 VLEWRFDSRL HLA-A*0201 (SEQ. ID NO.:294)HIV-1 nef 68-77 FPVTPQVPLR HLA-B7 (SEQ. ID NO.:295) HIV-1 nef 128-137TPGPGVRYPL HLA-B7 (SEQ. ID NO.:296) HIV-1 gagp24 308-316 QASQEVKNWHLA-Cw*0401 (SEQ. ID NO.:297) HIV-1 IIIB RT 273-282 VPLDEDFRKY HLA-B35(SEQ. ID NO.:298) HIV-1 IIIB RT 25-33 NPDIVIYQY HLA-B35 (SEQ. IDNO.:299) HIV-1 IIIB gp41 557-565 RAIEAQAHL HLA-B51 (SEQ. ID NO.:300)HIV-1 IIIB RT 231-238 TAFTIPSI HLA-B51 (SEQ. ID NO.:301) HIV-I IIIB pol215-223 VHPVHAGPIA HLA-B*5501 (SEQ. ID NO.:302) HIV-1 IIIB gp120 156-165NCSFNISTSI HLA-Cw8 (SEQ. ID NO.:303) HIV-I IIIB gp120 241-249 CTNVSTVQCHLA-Cw8 (SEQ. ID NO.:304) HIV-1 5F2 gp120 312-320 IGPGRAFHT H2-Dd (SEQ.ID NO.:305) HIV-1 5F2 pol 25-33 NPDIVIYQY HLA-B*3501 (SEQ. ID NO.:306)HIV-1 5F2 pol 432-441 EPIVGAETFY HLA-B*3501 (SEQ. ID NO.:307) HIV-1 5F2pol 432-440 EPIVGAETF HLA-B*3501 (SEQ. ID NO.:308) HLV-1 5F2 pol 6-14SPAIFQSSM HLA-B*3501 (SEQ. ID NO.:309) HIV-1 5F2 pol 59-68 VPLDKDFRKYHLA-B*3501 (SEQ. ID NO.:310) HIV-1 5F2 pol  6-14 IPLTEEAEL HLA-B*3501(SEQ. ID NO.:311) HlV-1 5F2 nef 69-79 RPQVPLRPMTY HLA-B*3501 (SEQ. IDNO.:312) HIV-1 5F2 nef 66-74 FPVRPQVPL HLA-B*3501 (SEQ. ID NO.:313)HIV-1 5F2 env 10-18 DPNPQEVVL HLA-B*3501 (SEQ. ID NO.:314) HIV-1 5F2 env 7-15 RPIVSTQLL HLA-B*3501 (SEQ. ID NO.:315) HIV-1 5F2 pol  6-14IPLTEEAEL HLA-B51 (SEQ. ID NO.:316) HIV-1 5F2 env 10-18 DPNPQEVVLHLA-B51 (SEQ. ID NO.:317) HIV-1 5F2 gagp24 199-207 AMQMLKETI H2-Kd (SEQ.ID NO.:318) HIV-2 gagp24 182-190 TPYDrNQML HLA-B*5301 (SEQ. ID NO.:319)HIV-2 gag 260-269 RRWIQLGLQKV HLA-B*2703 (SEQ. ID NO.:320) HIV-1 5F2gp41 593-607 GIWGCSGKLICTTAV HLA-B17 (SEQ. ID NO.:321) HIV-1 5F2 gp41753-767 ALIWEDLRSLCLFSY HLA-B22 (SEQ. ID NO.:322) HPV 6b E7 21-30GLHCYEQLV HLA-A*0201 (SEQ. ID NO.:323) HPV 6b E7 47-55 PLKQHFQIVHLA-A*0201 (SEQ. ID NO.:324) HPV11 E7  4-12 RLVTLKDIV HLA-A*0201 (SEQ.ID NO.:325) HPV16 E7 86-94 TLGIVCPIC HLA-A*0201 (SEQ. ID NO.:326) HPV16E7 85-93 GTLGIVCPI HLA-A*0201 (SEQ. ID NO.:327) HPV16 E7 12-20 MLDLQPETTHLA-A*0201 (SEQ. ID NO.:328) HPV16 E7 11-20 YMLDLQPETT HLA-A*0201 (SEQ.ID NO.:329) HPV16 E6 15-22 RPRKLPQL HLA-B7 (SEQ. ID NO.:330) HPV16 E649-57 RAHYNIVTF HW-Db (SEQ. ID NO.:331) HSV-1 gp B 498-505 SSIEFARLH2-Kb (SEQ. ID NO.:332) HSV-1 gp C 480-488 GIGIGVLAA HLA-A*0201 (SEQ. IDNO.:333) HSV-1 ICP27 448-456 DYATLGVGV H2-Kd (SEQ. ID NO.:334) HSV-1ICP27 322-332 LYRTFAGNPRA H2-Kd (SEQ. ID NO.:335) HSV-1 UL39 822-829QTFDFGRL H2-Kb (SEQ. ID NO.:336) HSV-2 gpC 446-454 GAGIGVAVL HLA-A*0201(SEQ. ID NO.:337) HLT V-i TAX 11-19 LLFGYPVYV HLA-A*0201 (SEQ. IDNO.:338) Influenza MP 58-66 GILGFVFTL HLA-A*0201 (SEQ. ID NO.:339)Influenza MP 59-68 ILGFVFTLTV HLA-A*0201 (SEQ. ID NO.:340) Influenza NP265-273 ILRGSVAHK HLA-A3 (SEQ. ID NO.:341) Influenza NP 91-99 KTGGPIYKRHLA-A*6801 (SEQ. ID NO.:342) Influenza NP 380-388 ELRSRYWAI HLA-B8 (SEQ.ID NO.:343) Influenza NP 381-388 LRSRYWAI HLA-B*2702 (SEQ. ID NO.:344)Influenza NP 339-347 EDLRVLSFI HLA-B*3701 (SEQ. ID NO.:345) InfluenzaNSI 158-166 GEISPLPSL HLA-B44 (SEQ. ID NO.:346) Influenza NP 338-346FEDLRVLSF HLA-B44 (SEQ. ID NO.:347) Influenza NSI 158-166 GEISPLPSLHLA-B*4402 (SEQ. ID NO.:348) Influenza NP 338-346 FEDLRVLSF HLA-B*4402(SEQ. ID NO.:349) Influenza PBI 591-599 VSDGGPKLY HLA-A1 (SEQ. IDNO.:350) Influenza A NP 44-52 CTELKLSDY HLA-A1 (SEQ. ID NO.:351)Influenza NSI 122-130 AIMDKNIIL HLA-A*0201 (SEQ. ID NO.:352) Influenza ANSI 123-132 IMDKNIILKA HLA-A*0201 (SEQ. ID NO.:353) Influenza A NP383-391 SRYWAIRTR HLA-B*2705 (SEQ. ID NO.:354) Influenza A NP 147-155TYQRTRALV H2-Kd (SEQ. ID NO.:355) Influenza A HA 210-219 TYVSVSTSTLH2-Kd (SEQ. ID NO.:356) Influenza A HA 518-526 IYSTVASSL H2-Kd (SEQ. IDNO.:357) Influenza A HA 259-266 FEANGNLI H2-Kk (SEQ. ID NO.:358)Influenza A HA 10-18 IEGGWTGMl H2-Kk (SEQ. ID NO.:359) Influenza A NP50-57 SDYEGRLI H2-Kk (SEQ. ID NO.:360) Influenza A NSI 152-160 EEGAIVGEIH2-Kk (SEQ. ID NO.:361) Influenza A34 NP 336-374 ASNENMETM H2Db (SEQ. IDNO.:362) Influenza A68 NP 366-374 ASNENMDAM H2Db (SEQ. ID NO.:363)Influenza B NP 85-94 KLGEFYNQMM HLA-A*0201 (SEQ. ID NO.:364) Influenza BNP 85-94 KAGEFYNQMM HLA-A*0201 (SEQ. ID NO.:365) Influenza JAP HA204-212 LYQNVGTYV H2Kd (SEQ. ID NO.:366) Influenza JAP HA 210-219TYVSVGTSTL H2-Kd (SEQ. ID NO.:367) Influenza JAP HA 523-531 VYQILATYAH2-Kd (SEQ. ID NO.:368) Influenza JAP HA 529-537 IYATVAGSL H2-Kd (SEQ.ID NO.:369) Influenza JAP HA 210-219 TYVSVGTSTI(L>I) H2-Kd (SEQ. IDNO.:370) Influenza JAP HA 255-262 FESTGNLI H2-Kk (SEQ. ID NO.:371) JHMVcAg 318-326 APTAGAFFF H2-Ld (SEQ. ID NO.:372) LCMV NP 118-126 RPQASGVYMH2-Ld (SEQ. ID NO.:373) (SEQ. ID NO.:374) LCMV NP 396-404 FQPQNGQFIH2-Db (SEQ. ID NO.:374) LCMV GP 276-286 SGVENPGGYCL H2-Db (SEQ. IDNO.:375) LCMV GP 33-42 KAVYNFATCG H2-Db (SEQ. ID NO.:376) MCMV pp89168-176 YPHFMPTNL H2-Ld (SEQ. ID NO.:377) MHV spike 510-518 CLSWNGPHLH2-Db protein (SEQ. ID NO.:378) MMTV env gp36 474-482 SFAVATTAL H2-Kd(SEQ. ID NO.:379) MMTV gagp27 425-433 SYETFISRL H2-Kd (SEQ. ID NO.:380)MMTV env gp73 544-551 ANYDFICV H2-Kb (SEQ. ID NO.:381) MuLV env p15E574-581 KSPWFTTL H2-Kb (SEQ. ID NO.:382) MuLV env gp70 189-196 SSWDFITVH2-Kb (SEQ. ID NO.:383) MuLV gag 75K 75-83 CCLCLTVFL H2-Db (SEQ. IDNO.:384) MuLV env gp70 423-431 SPSYVYHQF H2Ld (SEQ. ID NO.:385) MV Fprotein 437-447 SRRYPDAVYLH HLA-B*2705 (SEQ. ID NO.:386) Mv F protein438-446 RRYPDAVYL HLA-B*2705 (SEQ. ID NO.:387) Mv NP 281-289 YPALGLHEFH2-Ld (SEQ. ID NO.:388) Mv HA 343-351 DPVIDRLYL H2-Ld (SEQ. ID NO.:389)MV HA 544-552 SPGRSFSYF H2-Ld (SEQ. ID NO.:390) Poliovirus VP1 111-118TYKDTVQL H2-kd (SEQ. ID NO.:391) Poliovirus VP1 208-217 FYDGFSKVPL H2-Kd(SEQ. ID NO.:392) Pseudorabies G111 455-463 IAGIGILAI HLA-A*0201 virusgp (SEQ. ID NO.:393) Rabiesvirus NS 197-205 VEAEIAHQI H2-Kk (SEQ. IDNO.:394) Rotavirus VP7 33-40 llYRFLLl H2-Kb (SEQ. ID NO.:395) RotavirusVP6 376-384 VGPVFPPGM H2-Kb (SEQ. ID NO.:396) Rotavirus VP3 585-593YSGYIFRDL H2-Kb (SEQ. ID NO.:397) RSV M2 82-90 SYIGSINNI H2-Kd (SEQ. IDNO.:398) SIV gagp11C 179-190 EGCTPYDTNQML Mamu-A*01 (SEQ. ID NO.:399) SVNP 324-332 FAPGNYPAL H2-Db (SEQ. ID NO.:400) SV NP 324-332 FAPCTNYPALH2-Kb (SEQ. ID NO.:401) SV40 T 404-411 VVYDFLKC H2-Kb (SEQ. ID NO.:402)SV40 T 206-215 SAINNYAQKL H2-Db (SEQ. ID NO.:403) SV40 T 223-231CKGVNKEYL H2-Db (SEQ. ID NO.:404) SV40 T 489-497 QGINNLDNL H2-Db (SEQ.ID NO.:405) SV40 T 492-500 NNLDNLRDY(L) H2-Db (501) (SEQ. ID NO.:406)SV40 T 560-568 SEFLLEKRI H2-Kk (SEQ. ID NO.:407) VSV NP 52-59 RGYVYQGLH2-Kb (SEQ. ID NO.:408)

[0131] TABLE 5 HLA-A1 Position (Antigen) Source T cell EADPTGHSY MAGE-1161-169 epitopes (SEQ. ID NO.:409) VSDGGPNLY Influenza A PB (SEQ. IDNO.:410) 1591-599 CTELKLSDY Influenza A NP (SEQ. ID NO.:411) 44-52EVDPIGHLY MAGE-3 168-176 (SEQ. ID NO.:412) HLA-A201 MLLSVPLLLGCalreticulin signal (SEQ, ID NO.:413) sequence I-10 STBXQSGXQ HBV PRE-SPROTEIN (SEQ. ID NO.:414) 141-149 YMDGTMSQV Tyrosinase 369-377 (SEQ. IDNO.:415) ILKEPVHGV HIV - I RT 476-484 (SEQ. ID NO.:416) LLGFVFTLTVInfluenza MP 59-68 (SEQ. ID NO.:417) LLFGYPVYVV HTLV-1 tax 11-19 (SEQ.ID NO.:418) GLSPTVWLSV HBV sAg 348-357 (SEQ. ID NO.:419) WLSLLVPFV HBVsAg 335-343 (SEQ. ID NO.:420) FLPSDFFPSV HBV cAg 18-27 (SEQ. ID NO.:421)C L G 0 L L T M V EBVLMP-2426-434 (SEQ. ID NO.:422) FLAGNSAYEYV HCMV gp618-628B (SEQ. ID NO.:423) KLGEFYNQMM Influenza BNP 85-94 (SEQ. IDNO.:424) KLVALGINAV HCV-1 NS3 400-409 (SEQ. ID NO.:425) DLMGYIPLV HCV MP17-25 (SEQ. ID NO.:426) RLVTLKDIV HPV 11 EZ 4-12 (SEQ. ID NO.:427)MLLAVLYCL Tyrosinase 1-9 (SEQ. ID NO.:428) AAGIGILTV Melan A\Mart-127-35(SEQ. ID NO.:429) YLEPGPVTA Pmel 17/gp 100 480-488 (SEQ. ID NO.:430)ILDGTATLRL Pmel 17/gp 100 457-466 (SEQ. ID NO.:431) LLDGTATLRL Pmelgp1OO 457-466 (SEQ. ID NO.:432) ITDQVPFSV Pmel gp 100 209-217 (SEQ. IDNO.:433) KTWGQYWQV Pmel gp 100 154-162 (SEQ. ID NO.:434) TITDQVPFSV Pmelgp 100 208-217 (SEQ. ID NO.:435) AFHIIVAREL HIV-I nef 190-198 (SEQ. IDNO.:436) YLNKIQNSL P. falciparum CSP 334-342 (SEQ. ID NO.:437)MMRKLAILSV P. falciparum CSP 1-10 (SEQ. ID NO.:438) KAGEFYNQMM InfluenzaBNP 85-94 (SEQ. ID NO.:439) NIAEGLRAL EBNA-1 480-488 (SEQ. ID NO.:440)NLRRGTALA EBNA-1 519-527 (SEQ. ID NO.:441) ALAIPQCRL EBNA-1 525-533(SEQ. ID NO.:442) VLKDAIKDL EBNA-1 575-582 (SEQ. ID NO.:443) FMVFLQTHIEBNA-1 562-570 (SEQ. ID NO.:444) HLIVDTDSL EBNA-2 15-23 (SEQ. IDNO.:445) SLGNPSLSV EBNA-2 22-30 (SEQ. ID NO.:446) PLASAMRML EBNA-2126-134 (SEQ. ID NO.:447) RMLWMANYI EBNA-2 132-140 (SEQ. ID NO.:448)MLWMANYIV EBNA-2 133-141 (SEQ. ID NO.:449) ILPQGPQTA EBNA-2 151-159(SEQ. ID NO.:450) PLRPTAPTTI EBNA-2 171-179 (SEQ. ID NO.:451) PLPPATLTVEBNA-2 205-213 (SEQ. ID NO.:452) R M H L P V L H V EBNA-2 246-254 (SEQ.ID NO.:453) PMPLPPSQL EBNA-2 287-295 (SEQ. ID NO.:454) QLPPPAAPA EBNA-2294-302 (SEQ. ID NO.:455) SMPELSPVL EBNA-2 381-389 (SEQ. ID NO.:456)DLDESWDYl EBNA-2 453-461 (SEQ. ID NO.:457) P L P C V L W P VV BZLFl43-51 (SEQ. ID NO.:458) SLEECDSEL BZLFl 167-175 (SEQ. ID NO.:459)EIKRYKNRV BZLFI 176-184 (SEQ. ID NO.:460) QLLQFIYREV BZLFl 195-203 (SEQ.ID NO.:461) LLQHYREVA BZLFI 196-204 (SEQ. ID NO.:462) LLKQMCPSL BZLFI217-225 (SEQ. ID NO.:463) SIIPRTPDV BZLFI 229-237 (SEQ. ID NO.:464)AIMDKNIIL Influenza A NS1 122-130 (SEQ. ID NO.:465) IMDKNIILKA InfluenzaA NS1 123-132 (SEQ. ID NO.:466) LLALLSCLTV HCV MP 63-72 (SEQ. IDNO.:467) ILHTPGCV HCVMP 105-112 (SEQ. ID NO.:468) QLRRHIDLLV HCV env E66-75 (SEQ. ID NO.:469) DLCGSVFLV HCV env E 88-96 (SEQ. ID NO.:470)SMVGNWAKV HCV env E 172-180 (SEQ. ID NO.:471) HLHQNIVDV HCV NSI 308-316(SEQ. ID NO.:472) FLLLADARV HCV NSI 340-348 (SEQ. ID NO.:473)GLRDLAVAVEPVV HCV NS2 234-246 (SEQ. ID NO.:474) SLLAPGAKQNV HCV NS118-28 (SEQ. ID NO.:475) LLAPGAKQNV HCV NS1 19-28 (SEQ. ID NO.:476)FLLSLGIHL HBV pol 575-583 (SEQ. ID NO.:477) SLYADSPSV HBV pol 816-824(SEQ. ID NO.:478) GLSRYVARL HBV POL 455-463 (SEQ. ID NO.:479) KIFGSLAFLHER-2 369-377 (SEQ. ID NO.:480) ELVSEFSRM HER-2 971-979 (SEQ. IDNO.:481) KLTPLCVTL HIV-I gp 160 120-128 (SEQ. ID NO.:482) SLLNATDIAVHIV-I GP 160 814-823 (SEQ. ID NO.:483) VLYRYGSFSV Pmel gp100 476-485(SEQ. ID NO.:484) YIGEVLVSV Non-filament forming (SEQ. ID NO.:485) classI myosin family (HA-2)** LLFNILGGWV HCV NS4 192-201 (SEQ. ID NO.:486)LLVPFVQWFW HBV env 338-347 (SEQ. ID NO.:487) ALMPLYACI HBV pol 642-650(SEQ. ID NO.:488) YLVAYQATV HCV NS3 579-587 (SEQ. ID NO.:489) TLGIVCPICHIPV 16 E7 86-94 (SEQ. ID NO.:490) YLLPRRGPRL HCV core protein (SEQ. IDNO.:491) 34-43 LLPIFFCLWV HBV env 378-387 (SEQ. ID NO.:492) YMDDVVLGAHBV Pol 538-546 (SEQ. ID NO.:493) GTLGIVCPI HPV16 E7 85-93 (SEQ. IDNO.:494) LLALLSCLTI HCV MP 63-72 (SEQ. ID NO.:495) MLDLQPETT HPV 16 E712-20 (SEQ. ID NO.:496) SLMAFTAAV HCV NS4 174-182 (SEQ. ID NO.:497)CINGVCWTV HCV NS3 67-75 (SEQ. ID NO.:498) VMNILLQYVV Glutarnic acid(SEQ. ID NO.:499) decarboxylase 114-123 ILTVILGVL Melan A/Mart - 32-40(SEQ. ID NO.:500) FLWGPRALV MAGE-3 271-279 (SEQ. ID NO.:501) L L C P A GH A V HCV NS3 163-171 (SEQ. ID NO.:502) ILDSFDPLV HGV NSS 239-247 (SEQ.ID NO.:503) LLLCLIFLL HBV env 250-258 (SEQ. ID NO.:504) LIDYQGMLPV HBVenv 260-269 (SEQ. ID NO.:505) SIVSPFIPLL HBV env 370-379 (SEQ. IDNO;:506) FLLTRILTI HBV env 183-191 (SEQ. ID NO.:507) HLGNVKYLV P.faciparum TRAP (SEQ. ID NO.:508) 3-11 GIAGGLALL P. faciparum TRAP (SEQ.ID NO.:509) 500-508 ILAGYGAGV HCV NS S4A 236-244 (SEQ. ID NO.:510)GLQDCTMLV HCV NS5 714-722 (SEQ. ID NO.:511) TGAPVTYSTY HCV NS3 281-290(SEQ. ID NO.:512) VIYQYMDDLV HIV-1RT 179-187 (SEQ. ID NO.:513)VLPDVFIRCV N-acetylglucosaminyl- (SEQ. ID NO.:514) transferase V Gnt-Vintron VLPDVFIRC N-acetylglucosaminyl- (SEQ. ID NO.:515) transferase VGnt-V intron AVGIGIAVV Human CD9 (SEQ. ID NO.:516) LVVLGLLAV Humanglutamyl- (SEQ. ID NO.:517) transferase ALGLGLLPV Human G proteincoupled receptor (SEQ. ID NO.:518) 164-172 GIGIGVLAA HSV-I gp C 480-488(SEQ. ID NO.:519) GAGIGVAVL HSV-2 gp C 446-454 (SEQ. ID NO.:520)IAGIGILAI Pseudorabies gpGN (SEQ. ID NO.:521) 455-463 LIVIGILILAdenovirus 3 E3 9kD (SEQ. ID NO.:522) 30-38 LAGIGLIAA S. LincolnensisImrA (SEQ. ID NO.:523) VDGIGILTI Yeast ysa-1 77-85 (SEQ. ID NO.:524)GAGIGVLTA B. polymyxa, (SEQ. ID NO.:525) βcndoxylanase 149-157 157AAGIGIIQI E. coli methionine (SEQ. ID NO.:526) synthase 590-598QAGIGILLA E. coli hypothetical (SEQ. ID NO.:527) protein 4-12KARDPHSGHFV CDK4w1 22-32 (SEQ. ID NO.:528) KACDPI-ISGIIFV CDK4-R24C22-32 (SEQ. ID NO.:529) ACDPFISGHFV CDK4-R24C 23-32 (SEQ. ID NO.:530)SLYNTVATL HIV-I gag p 17 77-85 (SEQ. ID NO.:531) ELVSEFSRV HER-2, m>V(SEQ. lD NO.:532) substituted 971-979 RGPGRAFVTI HIV-I gp 160 315-329(SEQ. ID NO.:533) HMWNFISGI HCV NS4A 149-157 (SEQ. ID NO.:534)NLVPMVATVQ HCMV pp65 495-504 (SEQ. ID NO.:535) GLHCYEQLV HPV 6b E7 21-30(SEQ. ID NO.:536) PLKQHFQIV HPV 6b E7 47-55 (SEQ. ID NO.:537) LLDFVRFMGVEBNA-6 284-293 (SEQ. ID NO.:538) AIMEKNIML Influenza Alaska NS 1 (SEQ.ID NO.:539) 122-130 YLKTIQNSL P. falciparum cp36 (SEQ. ID NO.:540) CSPYLNKIQNSL P. falciparum cp39 (SEQ. ID NO.:541) CSP YMLDLQPETT HPV 16 E711-20* (SEQ. ID NO.:542) LLMGTLGIV HPV 16 E7 82-90** (SEQ. ID NO.:543)TLGIVCPI HPV 16 E7 86-93 SEQ ID NO.:544 TLTSCNTSV HIV-1 gp120 197-205(SEQ. ID NO.:545) KLPQLCTEL HPV 16 E6 18-26 (SEQ. ID NO.:546) TIHDIILECHPV16 E6 29-37 (SEQ. ID NO.:547) LGIVCPICS HPV16 E7 87-95 (SEQ. IDNO.:548) VILGVLLLI Melan A/Mart-1 35-43 (SEQ. ID NO.:549) ALMDKSLHVMelan A/Mart-1 56-64 (SEQ. ID NO.:550) GILTVILGV Melan A/Mart-1 31-39(SEQ. ID NO.:551) T cell MINAYLDKL P. Falciparum STARP epitopes (SEQ. IDNO.:552) 523-531 AAGIGILTV Melan A/Mart-1 27-35 (SEQ. ID NO.:553)FLPSDFFPSV HBV cAg 18-27 (SEQ. ID NO.:554) Motif SVRDRLARL EBNA-3464-472 unknown (SEQ. ID NO.:555) T cell epitopes T cell AAGIGILTV MelanA/Mart-1 27-35 epitopes (SEQ. ID NO.:556) FAYDGKDYI Human MHC I-ot (SEQ.ID NO.:557) 140-148 T cell AAGIGILTV Melan A/Mart-1 27-35 epitopes (SEQ.ID NO.:558) FLPSDFFPSV HBV cAg 18-27 (SEQ. ID NO.:559) Motif AAGIGILTVMeland A/Mart-1 27-35 unknown (SEQ. ID NO.:560) T cell epitopesFLPSDFFPSV HBV cAg 18-27 (SEQ. ID NO.:561) AAGIGILTV Melan A/Mart-127-35 (SEQ. ID NO.:562) ALLAVGATK Pmel17 gp 100 17-25 (SEQ. ID NO.:563)T cell R L R D L L L I V T R HIV-1 gp41 768-778 epitopes (SEQ. IDNO.:564) QVPLRPMTYK HIV-1 nef 73-82 (SEQ. ID NO.:565) TVYYGVPVWK HIV-1gp120 - 36-45 (SEQ. ID NO.:566) RLRPGGKKK HIV-1 gag p 17 20-29 (SEQ. IDNO.:567) ILRGSVAHK Influenza NP 265-273 (SEQ. ID NO.:568) RLRAEAGVKEBNA-3 603-611 (SEQ. ID NO.:569) RLRDLLLIVTR HIV-1 gp41 770-780 (SEQ. IDNO.:570) VYYGVPVWK HIV-I GP 120 38-46 (SEQ. ID NO.:571) RVCEKMALY HCVNS5 575-583 (SEQ. ID NO.:572) Motif KIFSEVTLK Unknown; muta unknown(SEQ. ID NO.:573) melanoma peptide ted T cell (p I 83L) 175-183 epitopeYVNVNMGLK* HBV cAg 88-96 (SEQ. ID NO.:574) T cell IVTDFSVIK EBNA-4416-424 epitopes (SEQ. ID NO.:575) ELNEALELK P53 343-351 (SEQ. IDNO.:576) VPLRPMTYK HIV-1 NEF 74-82 (SEQ. ID NO.:577) AIFQSSMTK HIV-Igagp24 325-333 (SEQ. ID NO.:578) QVPLRPMTYK HIV-1 nef 73-82 (SEQ. IDNO.:579) TINYTIFK HCV NSI 238-246 (SEQ. ID NO.:580) AAVDLSHFLKEK HIV-1nef 83-94 (SEQ. ID NO.:581) ACQ G V G G P G G H K HIV-1 II 1B p24 (SEQ.ID NO.:582) 349-359 HLA-A24 S Y L D S G I H F* β-catenin, mutated (SEQ.ID NO.:583) (proto-onocogen) 29-37 T cell RYLKDQQLL HIV GP 41 583-591epitopes (SEQ. ID NO.:584) AYGLDFYIL P15 melanoma Ag 10-18 (SEQ. IDNO.:585) AFLPWHRLFL Tyrosinase 206-215 (SEQ. ID NO.:586) AFLPWHRLFTyrosinase 206-214 (SEQ. ID NO.:587) RYSIFFDY Ebna-3 246-253 (SEQ. IDNO.:588) T cell ETINEEAAEW HIV-1 gagp24 203-212 epitope (SEQ. IDNO.:589) T cell STLPETTVVRR HBV cAg 141-151 epitopes (SEQ. ID NO.:590)MSLQRQFLR ORF 3P-gp75 294-321 (SEQ. ID NO.:591) (bp) LLPGGRPYR TRP(tyrosinase rel.) (SEQ. ID NO.:592) 197-205 T cell IVGLNKIVR HIV gagp24epitope (SEQ. ID NO.:593) 267-267-275 AAGIGILTV Melan A/Mart-1 27 35(SEQ. ID NO.:594)

[0132] Table 6 sets forth additional antigens useful in the inventionthat are available from the Ludwig Cancer Institute. The Table refers topatents in which the identified antigens can be found and as such areincorporated herein by reference. TRA refers to the tumor-relatedantigen and the LUD No. refers to the Ludwig Institute number. TABLE 6TRA LUD No. Patent No. Date Patent Issued Peptide (Antigen) HLA MAGE-45293 5,405,940 11 Apr. 1995 EVDPASNTY HLA-A1 (SEQ. ID NO.:979) MAGE-415293 5,405,940 11 Apr. 1995 EVDPTSNTY HLA-AI (SEQ ID NO:595) MAGE-5 52935,405,940 11 Apr. 1995 EADPTSNTY HLA-AI (SEQ ID NO:596) MAGE-51 52935,405,940 11 Apr. 1995 EADPTSNTY HLA-AI (SEQ ID NO:597) MAGE-6 52945,405,940 11 Apr. 1995 EVDPIGHVY HLA-A1 (SEQ ID NO:598) 5299.2 5,487,97430 Jan. 1996 MLLAVLYCLL HLA-A2 (SEQ ID NO:599) 5360 5,530,096 25 Jun.1996 MLLAVLYCL HLA-B44 (SEQ ID NO:600) Tyrosinase 5360.1 5,519,117 21May 1996 SEIWRDIDFA HLA-B44 (SEQ ID NO:601) SEIWRDIDF (SEQ ID NO:602)Tyrosinase 5431 5,774,316 28 Apr. 1998 XEIWRDIDF HLA-B44 (SEQ ID NO:603)MAGE-2 5340 5,554,724 10 Sep. 1996 STLVEVTLGEV HLA-A2 (SEQ ID NO:604)LVEVTLGEV (SEQ ID NO:605) VIFSKASEYL (SEQ ID NO:606) IIVLAIIAl (SEQ IDNO:607) KIWEELSMLEV (SEQ ID NO:608) LIETSYVKV (SEQ ID NO:609) 53275,585,461 17 Dec. 1996 FLWGPRALV HLA-A2 (SEQ ID NO:610) TLVEVTLGEV (SEQID NO:611) ALVETSYVKV (SEQ ID NO:612) MAGE-3 5344 5,554,506 10 Sep. 1996KIWEELSVL HLA-A2 (SEQ ID NO:613) MAGE-3 5393 5,405,940 11 Apr. 1995EVDPIGHLY HLA-A1 (SEQ ID NO:614) MAGE 5293 5,405,940 11 Apr. 1995 EXDX5YHLA-A1 (SEQ. ID NO.:615) (but not EADPTGHSY) SEQ. ID NO.:616) E (A/V) DX5 Y (SEQ. ID NO.:617) E (A/V) D P X4 Y (SEQ. ID NO.:618) E (A/V) D P(I/A/T) X3 Y (SEQ. ID NO.:619) E (A/V) D P (I/A/T) (G/S) X2 Y (SEQ. IDNO.:620) E (A/V) D P (I/A/T) (G/S) (H/N) X Y (SEQ. ID NO.:621) E (A/V)DP (I/A/T) (G/S) (H/N) (L/T/V) Y (SEQ. 11) NO.:622) MAGE-1 53615,558,995 24 Sep. 1996 ELHSAYGEPRKLLTQD HLA-C (SEQ ID NO:623) Clone 10EHSAYGEPRKLL (SEQ ID NO:624) SAYGEPRKL (SEQ ID NO:625) MAGE-1 5253.4 TBATBA EADPTGHSY HLA-AI (SEQ ID NO:626) BAGE 5310.1 TBA TBAMAARAVFLALSAQLLQARLMKE HLA-C (SEQ ID NO:627) Clone 10 MAARAVFLALSAQLLQHLA-C (SEQ ID NO:628) Clone 10 AARAVFLAL HLA-C (SEQ ID NO:629) Clone 10GAGE 5323.2 5,648,226 15 Jul. 1997 YRPRPRRY HLA-CW6 (SEQ. ID NO.:630)

[0133] TABLE 7 T cell epitope AA MHC MHC ligand SEQ. Source ProteinPosition molecules (Antigen) ID NO.: Ref. synthetic synthetic syntheticHLA-A2 ALFAAAAAV 631 Parker, et al., “Scheme for peptides peptidespeptides ranking potential HLA-A2 binding peptides based on independentbinding of individual peptide side- chains,” J. Immunol. 152:163-175GIFGGVGGV 632 Parker, et al., “Scheme for ranking potential HLA-A2binding peptides based on independent binding of individual peptideside- chains,” J. Immunol. 152:163-175 GLDKGGGV 633 Parker, et al.,“Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGFGGV 634 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGGAGV 635 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGEGV 636 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGGFGV 637 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGGGL 638 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGGGGV 639 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGVGV 640 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGVGGV 641 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGVGKV 642 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFKGVGGV 643 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLGGGGFGV 644 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLLGGGVGV 645 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLYGGGGGV 646 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GMFGGGGGV 647 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GMFGGVGGV 648 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GQFGGVGGV 649 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GVFGGVGGV 650 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 KLFGGGGGV 651 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 KLFGGVGGV 652 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 AILGFVFTL 653 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GAIGFVFTL 654 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GALGFVFTL 655 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GELGFVFTL 656 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GIAGFVFTL 657 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GIEGFVFTL 658 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILAFVFTL 659 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILGAVFTL 660 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILGEVFTL 661 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILFGAFTL 662 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILGFEFTL 663 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILGFKFTL 664 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILGFVATL 665 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILGFVETL 666 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILGFVFAL 667 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILGFVFEL 668 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILGFVFKL 669 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILGFVFTA 670 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILGFVFTL 671 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILGFVFVL 672 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILGFVKTL 673 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILGKVFTL 674 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GILKFVFTL 675 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GILPFVFTL 676 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GIVGFVFTL 677 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GKLGFVFTL 678 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLLGFVFTL 679 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GQLGFVFTL 680 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 KALGFVFTL 681 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 KILGFVFTL 682 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 KILGKVFTL 683 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 AILLGVFML 684 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 AIYKRWIIL 685 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 ALFFFDIDL 686 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 ATVELLSEL 687 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 CLFGYPVYV 688 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 FIFPNYTIV 689 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 IISLWDSQL 690 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 ILASLFAAV 691 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 ILESLFAAV 692 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 KLGEFFNQM 693 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 KLGEFYNQM 694 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 LLFGYPVYV 695 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 LLWKGEGAV 696 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 LMFGYPVYV 697 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 LNFGYPVYV 698 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 LQFGYPVYV 699 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 NIVAHTFKV 700 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 NLPMVATV 701 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 QMLLAIARL 702 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 QMWQARLTV 703 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 RLLQTGIHV 704 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 RLVNGSLAL 705 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 SLYNTVATL 706 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 TLNAWVKVV 707 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 WLYRETCNL 708 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 YLFKRMIDL 709 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GAFGGVGGV 710 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GAFGGVGGY 711 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GEFGGVGGV 712 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GGFGGVGGV 713 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GIFGGGGGV 714 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GIGGFGGGL 715 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GIGGGGGGL 716 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLDGGGGGV 717 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLDGKGGGV 718 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLDKKGGGV 719 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGFGF 720 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGGFGG 721 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGFGN 722 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGGFGS 723 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGGGI 724 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGGGGM 725 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGGGT 726 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLFGGGGGY 727 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLGFGGGGV 728 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLGGFGGGV 729 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLGGGFGGV 730 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLGGGGGFV 731 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLGGGGGGY 732 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLGGGVGGV 733 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLLGGGGGV 734 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GLPGGGGGV 735 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GNFGGVGGV 736 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GSFGGVGGV 737 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GTFGGVGGV 738 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 AGNSAYEYV 739 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFPGQFAY 740 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 HILLGVFML 741 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 ILESLFRAV 742 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 KKKYKLKHI 743 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 MLASIDLKY 744 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 MLERELVRK 745 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 KLFGFVFTV 746 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 ILDKKVEKV 747 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 ILKEPVHGV 748 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 ALFAAAAAY 749 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GIGFGGGGL 750 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GKFGGVGGV 751 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GLFGGGGGK 752 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 EILGFVFTL 753 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 GIKGFVFTL 754 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 GQLGFVFTK 755 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 ILGFVFTLT 756 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 KILGFVFTK 757 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 KKLGFVFTL 758 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 KLFEKVYNY 759 Parker, etal., “Scheme for ranking potential HLA-A2 binding peptides based onindependent binding of individual peptide side- chains,” J. Immunol.152:163-175 LRFGYPVYV 760 Parker, et al., “Scheme for ranking potentialHLA-A2 binding peptides based on independent binding of individualpeptide side- chains,” J. Immunol. 152:163-175 Human HSP60 140-148HLA-B27 IRRGVMLAV 761 Rammensee et al. 1997 160 ″ ″ 369-377 ″ KRIQEIIEQ762 Rammensee et al. 1997 160 ″ ″ 469-477 ″ KRTLKIPAM 763 Rammensee etal. 1997 160 Yersinia HSP6O 35-43 GRNVVLDKS 764 Rammensee et al. 1997160 ″ ″ 117-125 KRGIDKAVI 765 Rammensee et al. 1997 160 ″ ″ 420-428IRAASAITA 766 Rammensee et al. 1997 160 ″ HSP 60 284-292 HLA- RRKAMFEDI767 169 B*2705 P. LSA-1 1850-1857 HLA-B3501 KPKDELDY 768 170 falciparumInfluenza 379-387 HLA- LELRSRYWA 769 183 NP B*4402 Tum-P35B 4-13HLA-D^(d) GPPHSNNFGY 770 230 Rotavirus VP7 33-40 IIYRFLLI 771 262 OGDH104-112 H2-L^(d) QLSPYPFDL 772 253 (F108Y) TRP-2 181-188 p287 VYDFFVWL773 284 DEAD box 547-554 p287 SNFVFAGI 774 283 p 68 Vector p287 SVVEFSSL775 260 “artefact” Epitope p287 AHYLFRNL 776 278 mimic of tumor Ag ″THYLFRNL 777 ″ Epitope mimic ″ LIVIYNTL 778 279 of H-3 miHAg” ″ LIYEFNTL779 ″ ″ IPYIYNTL 780 ″ ″ IIYIYHRL 781 ″ ″ LIYIFNTL 782 ″ HBV cAg  93-100″ MGLKFRQL 783 280 Human autoantigen 51-58 ″ IMIKFRNRL 784 281 LA MouseUTY protein H2D^(b) WMHHNMDLI 785 303 Mouse p53 232-240 ″ KYMCNSSCM 786302 MURINE MDM2 441-449 ″ GRPKNGCIV 787 277 Epitope mimic ″ AQHPNAELL788 278 of natural MuLV 75-83 ″ CCLCLTVFL 789 301 gag75K P. CSP 375-383p290 YENDIEKK 790 315 Falciparum P. ″ 371-379 ″ DELDYENDI 791 315Falciparum HIV −1RT 206-214 ″ TEMEKEGKI 792 316 Rabies NS 197-205VEAEIAHQI 793 309, 310 Influenza NS1 152-160 ″ EEGAIVGEI 794 304 AMurine SMCY p291 TENSGKDI 795 317 MHC class  3-11 p293 AMAPRTLLL 796 3181 leader ND1alpha  1-12 p293 FFINILTLLVP 797 323 ND Beta  1-12 p293FFINILTLLVP 798 323 ND alpha  1-17 ″ FFINILTLLVPI 799 324 LIAM ND Beta 1-17 ″ FFINALTLLVPI 800 ″ LIAM COI 1-6 ″ FINRW 801 325 mitochondrial L.LemA 1-6 ″ IGWII 802 326 monocyto- genes SIV gag 179-190 Mamu-EGCTPYDINQ 803 334 p11C A*01 ML MAGE-3 HLA-A2 ALSRKVAEL 804 5,554,506   ″ IMPKAGLLI 805 ″ ″ KIWEELSVL 806 ″ ″ ALVETSYVKV 807 ″ ″ ThrLeuValGluVal808 ″ ThrLeuGlyGluVal ″ AlaLeuSerArgLys 809 ″ ValAlaGluLeu ″IleMetProLysAla 810 ″ GlyLeuLeuIle ″ LysIleTrpGluGlu 811 ″ LeuSerValLeu″ AlaLeuValGluThr 812 ″ SerTyrValLysVal peptides HLA-A2 Lys Gly Ile Leu813 5,989,565    which bind Gly Phe Val Phe to MHCs Thr Leu Thr Val ThrLeu Thr Val ″ Gly Ile Ile Gly 814 ″ Phe Val Phe Thr Ile ″ Gly Ile IleGly 815 ″ Phe Val Phe Thr Leu ″ Gly Ile Leu Gly 816 ″ Phe Val Phe ThrLeu ″ Gly Leu Leu Gly 817 ″ Phe Val Phe Thr Leu ″ XXTVXXGVX, 818 ″ X =Leu or Ile (6-37) ″ Ile Leu Thr Val 819 ″ Ile Leu Gly Val Leu ″ Tyr LeuGlu Pro 820 ″ Gly Pro Val Thr Ala ″ Gln Val Pro Leu 821 ″ Arg Pro MetThr Tyr Lys ″ Asp Gly Leu Ala 822 ″ Pro Pro Gln His Leu Ile Arg ″ LeuLeu Gly Arg 823 ″ Asn Ser Phe Glu Val Peptides from HLA-CGluHisSerAlaTyr 824 5,558,995    MAGE-1 clone 10 GlyGluProArgLysLeuLeuThrGlnAsp Leu HLA-C GluHisSerAlaTyr 825 ″ clone 10 GlyGluProArgLysLeuLeuThrGlnAsp Leu HLA-C SerAlaTyrGlyGlu 826 ″ clone 10 ProArgLysLeuGAGE HLA-Cw6 TyrArgProArgPro 827 5,648,226 ‘  ArgArgTyr ″ThrTyrArgProArg 828 ″ ProArgArgTyr ″ TyrArgProArgPro 829 ″ ArgArgTyrVal″ ThrTyrArgProArg 830 ″ ProArgArgTyrVal ″ ArgProArgProArg 831 ″ArgTyrValGlu ″ MetSerTrpArgGly 832 ″ ArgSerThrTyrArg ProArgProArgArg ″ThrTyrArgProArg 833 ″ ProArgArgTyrVal GluProProGluMet Ile MAGE HLA-A1,Isolated nonapeptide 834 5,405,940    primarily having Glu at its Nterminal, Tyr at its C-terminal, and Asp at the third residue from its Nterminal, with the proviso that said isolated nonapeptide is not Glu AlaAsp Pro Thr Gly His Ser Tyr (SEQ ID NO: 1), and wherein said isolatednona- peptide binds to a human leukocyte antigen molecule on a cell toform a complex, said complex provoking lysis of said cell by a cytolyticT cell specific to said complex HLA-A1, GluValValProIle 835 ″ primarilySerHisLeuTyr HLA-A1, GluValValArgIle 836 ″ primarily GlyHisLeuTyrHLA-A1, GluValAspProIle 837 ″ primarily GlyHisLeuTyr HLA-A1,GluValAspProAla 838 ″ primarily SerAsnThrTyr HLA-A1, GluValAspProThr 839″ primarily SerAsnThrTyr HLA-A1, GluAlaAspProThr 840 ″ primarilySerAsnThrTyr HLA-A1, GluValAspProIle 841 ″ primarily GlyHisValTyr ″HLA-A1, GAAGTGGTCC 842 ″ primarily CCATCAGCCA CTTGTAC HLA-A1, GAAGTGGTCC843 ″ primarily GCATCGGCCA CTTGTAC HLA-A1, GAAGTGGAC 844 ″ primarilyCCCATCGGCC ACTTGTAC HLA-A1, GAAGTGGAC 845 ″ primarily CCCGCCAGCAACACCTAC HLA-A1, GAAGTGGAC 846 ″ primarily CCCACCAGCA ACACCTAC HLA-A1,GAAGCGGAC 847 ″ primarily CCCACCAGCA ACACCTAC HLA-A1, GAAGCGGAC 848 ″primarily CCCACCAGCA ACACCTAC HLA-A1, GAAGTGGAC 849 ″ primarilyCCCATCGGCC ACGTGTAC HLA-A1, GluAlaAspProThr 850 ″ primarily GlyHisSerHLA-A1, AlaAspProTrpGly 851 ″ primarily HisSerTyr MAGE peptides HLA-A2SerThrLeuValGlu 852 5,554,724    ValThrLeuGly GluVal ″ ″ LeuValGluValThr853 ″ LeuGlyGluVal ″ ″ LysMetValGluLeu 854 ″ ValHisPheLeu ″ ″ValIlePheSerLys 855 ″ AlaSerGluTyrLeu ″ ″ TyrLeuGlnLeuVal 856 ″PheGlyIleGluVal ″ ″ GlnLeuValPheGly 857 ″ IleGluValVal ″ ″GlnLeuValPheGly 858 ″ IleGluValValGlu Val ″ ″ IleIleValLeuAla 859 ″IleIleAlaIle ″ ″ LysIleTrpGluGlu 860 ″ LeuSerMetLeuGlu Val ″ ″AlaLeuIleGluThr 861 ″ SerTyrValLysVal ″ ″ LeuIleGluThrSer 862 ″TyrValLysVal ″ ″ GlyLeuGluAlaArg 863 ″ GlyGluAlaLeuGly GlyLeu ″ ″GlyLeuGluAlaArg 864 ″ GlyGluAlaLeu ″ ″ AlaLeuGlyLeuVal 865 ″GlyAlaGlnAla ″ ″ GlyLeuValGlyAla 866 ″ GlnAlaProAla ″ ″ AspLeuGluSerGlu867 ″ PheGlnAlaAla ″ ″ AspLeuGluSerGlu 868 ″ PheGlnAlaAlaIle ″ ″AlaIleSerArgLys 869 ″ MetValGluLeuVal ″ ″ AlaIleSerArgLys 870 ″MetValGluLeu ″ ″ LysMetValGluLeu 871 ″ ValHisPheLeuLeu ″ ″LysMetValGluLeu 872 ″ ValHisPheLeu LeuLeu ″ ″ LeuLeuLeuLysTyr 873 ″ArgAlaArgGlu ProVal ″ ″ LeuLeuLysTyrArg 874 ″ AlaArgGluProVal ″ ″ValLeuArgAsnCys 875 ″ GlnAspPhePhe ProVal ″ ″ TyrLeuGlnLeuVal 876 ″PheGlyIleGlu ValVal ″ ″ HisLeuTyrIleLeu 879 ″ ValThrCysLeu ″ ″HisLeuTyrIleLeu 880 ″ ValThrCysLeuGly Leu ″ ″ TyrIleLeuValThr 881 ″CysLeuGlyLeu CysLeuGlyLeuSer 882 ″ TyrAspGlyLeu ″ ″ CysLeuGlyLeuSer 883″ TyrAspGlyLeuLeu ″ ″ ValMetProLysThr 884 ″ GlyLeuLeuIle ″ ″ValMetProLysThr 885 ″ GlyLeuLeuIleIle ″ ″ ValMetProLysThr 886 ″GlyLeuLeuIleIle Val ″ ″ GlyLeuLeuIleIle 887 ″ ValLeuAlaIle ″ ″GlyLeuLeuIleIle 888 ″ ValLeuAlaIleIle ″ ″ GlyLeuLeuIleIle 889 ″ValLeuAlaIleIle Ala ″ ″ LeuLeuIleIleVal 890 ″ LeuAlaIleIle ″ ″LeuLeuIleIleVal 891 ″ LeuAlaIleIleAla ″ ″ LeuLeuIleIleVal 892 ″LeuAlaIleIleAlaIle ″ ″ LeuIleIleValLeu 893 ″ AlaIleIleAla ″ ″LeuIleIleValLeu 894 ″ AlaIleIleAlaIle ″ ″ IleIleAlaIleGluGly 895 ″AspCysAla ″ ″ LysIleTrpGluGlu 896 ″ LeuSerMetLeu ″ ″ LeuMetGlnAspLeu 897″ ValGlnGluAsn TyrLeu ″ ″ PheLeuTrpGlyPro 898 ″ ArgAlaLeuIle ″ ″LeuIleGluThrSer 899 ″ TyrValLysVal ″ ″ AlaLeuIleGluThr 900 ″SerTyrValLysVal Leu ″ ″ ThrLeuLysIleGly 901 ″ GlyGluProHisIle ″ ″HisIleSerTyrPro 902 ″ ProLeuHisGluArg Ala ″ ″ GlnThrAlaSerSer 903 ″SerSerThrLeu ″ ″ GlnThrAlaSerSer 904 ″ SerSerThrLeuVal ″ ″ValThrLeuGlyGlu 905 ″ ValProAlaAla ″ ″ ValThrLysAlaGlu 906 ″MetLeuGluSerVal ″ ″ ValThrLysAlaGlu 907 ″ MetLeuGluSer ValLeu ″ ″ValThrCysLeuGly 908 ″ LeuSerTyrAsp GlyLeu ″ ″ LysThrGlyLeuLeu 909 ″IleIleValLeu ″ ″ LysThrGlyLeuLeu 910 ″ IleIleValLeuAla ″ ″LysThrGlyLeuLeu 911 ″ IleIleValLeuAla Ile ″ ″ HisThrLeuLysIle 912 ″GlyGlyGluProHis Ile ″ ″ MetLeuAspLeu 913 ″ GlnProGluThrThr Mage-3 HLA-A2GlyLeuGluAlaArg 914 5,585,461    peptides GlyGluAlaLeu Mage-3 ″AlaLeuSerArgLys 915 ″ peptides ValAlaGluLeu Mage-3 ″ PheLeuTrpGlyPro 916″ peptides ArgAlaLeuVal Mage-3 ″ ThrLeuValGluVal 917 ″ peptidesThrLeuGlyGluVal Mage-3 ″ AlaLeuSerArgLys 918 ″ peptides ValAlaGluLeuValMage-3 ″ AlaLeuValGluThr 919 ″ peptides SerTyrValLysVal TyrosinaseHLA-A2 TyrMetAsnGlyThr 920 5,487,974    MetSerGlnVal ″ MetLeuLeuAlaVal921 ″ LeuTyrCysLeuLeu Tyrosinase HLA-A2 MetLeuLeuAlaVal 922 5,530,096   LeuTyrCysLeu ″ ″ LeuLeuAlaValLeu 923 ″ TyrCysLeuLeu Tyrosinase HLA-A2and SerGluIleTrpArg 924 5,519,117    HLA-B44 AspIleAspPheAla HisGluAla ″HLA-A2 and SerGluIleTrpArg 925 ″ HLA-B44 AspIleAspPhe ″ HLA-A2 andGluGluAsnLeuLeu 926 ″ HLA-B44 AspPheValArg Phe Melan EAAGIGILTV 927Jäger, E. et al. A/MART-1 Granulocyte-macrophage- colony-stimulatingFactor Enhances Immune Responses To Melanoma-′associated Peptides invivo Int. J Cancer 67, 54-62 (1996) Tyrosinase MLLAVLYCL 928 Jäger, E.et al. Granulocyte-macrophage- colony-stimulating Factor Enhances ImmuneResponses To Melanoma-′associated Peptides in vivo Int. J Cancer 67,54-62 (1996) ″ YMDGTMSQV 929 Jäger, E. et al. Granulocyte-macrophage-colony-stimulating Factor Enhances Immune Responses ToMelanoma-′associated Peptides in vivo Int. J Cancer 67, 54-62 (1996)gp100/Pme YLEPGPVTA 930 Jäger, E. et al. 117 Granulocyte-macrophage-colony-stimulating Factor Enhances Immune Responses ToMelanoma-′associated Peptides in vivo Int. J Cancer 67, 54-62 (1996)gp100/Pme LLDGTATLRL 931 Jäger, E. et al. 117 Granulocyte-macrophage-colony-stimulating Factor Enhances Immune Responses ToMelanoma-′associated Peptides in vivo Int. J Cancer 67, 54-62 (1996)Influenza GILGFVFTL 932 Jäger, E. et al. matrix Granulocyte-macrophage-colony-stimulating Factor Enhances Immune Responses ToMelanoma-′associated Peptides in vivo Int. J Cancer 67, 54-62 (1996)MAGE-1 EADPTGHSY 933 Jäger, E. et al. Granulocyte-macrophage-colony-stimulating Factor Enhances Immune Responses ToMelanoma-′associated Peptides in vivo Int. J Cancer 67, 54-62 (1996)MAGE-1 HLA-A1 EADPTGHSY 934 BAGE HLA-C MAARAVFLAL 935 Jäger, E. et al.SAQLLQARLM Granulocyte-macrophage- KE colony-stimulating Factor EnhancesImmune Responses To Melanoma-′associated Peptides in vivo Int. J Cancer67, 54-62 (1996) ″ ″ MAARAVFLAL 936 Jäger, E. et al. SAQLLQGranulocyte-macrophage- colony-stimulating Factor Enhances ImmuneResponses To Melanoma-′associated Peptides in vivo Int. J Cancer 67,54-62 (1996) ″ ″ AARAVFLAL 937 Jäger, E. et al. Granulocyte-macrophage-colony-stimulating Factor Enhances Immune Responses ToMelanoma-′associated Peptides in vivo Int. J Cancer 67, 54-62 (1996)Influenza PRS NP 147-154 K^(d) IYQRIRALV 938 Falk et al., Allele-specific motifs revealed by sequencing of self- peptides eluted from MHCmolecules SELF P815 ″ SYFPEITHI 939 Falk et al., Allele- PEPTIDEspecific motifs revealed by sequencing of self- peptides eluted from MHCmolecules Influenza Jap HA ″ IYATVAGSL 940 Falk et al., Allele- 523-549specific motifs revealed by sequencing of self- peptides eluted from MHCmolecules ″ Jap HA ″ VYQILAIYA 941 Falk et al., Allele- 523-549 specificmotifs revealed by sequencing of self- peptides eluted from MHCmolecules ″ Jap HA ″ IYSTVASSL 942 Falk et al., Allele- 523-549 specificmotifs revealed by sequencing of self- peptides eluted from MHCmolecules ″ JAP HA ″ LYQNVGTYV 943 Falk et al., Allele- 202-221 specificmotifs revealed by sequencing of self- peptides eluted from MHCmolecules HLA-A24 ″ RYLENQKRT 944 Falk et al., Allele- specific motifsrevealed by sequencing of self- peptides eluted from MHC moleculesHLA-Cw3 ″ RYLKNGKET 945 Falk et al., Allele- specific motifs revealed bysequencing of self- peptides eluted from MHC molecules P815 ″ KYQAVTTTL946 Falk et al., Allele- specific motifs revealed by sequencing of self-peptides eluted from MHC molecules Plasmodium CSP ″ SYIPSAEKI 947 Falket al., Allele- berghei specific motifs revealed by sequencing of self-peptides eluted from MHC molecules Plasmodium CSP ″ SYVPSAFQI 948 Falket al., Allele- yoehi specific motifs revealed by sequencing of self-peptides eluted from MHC molecules Vesicular NP 52-59 K^(b) RGYVYQGL 949Falk et al., Allele- stomatitis specific motifs revealed viruse bysequencing of self- peptides eluted from MHC molecules Ovalbumin ″SIINFEKL 950 Falk et al., Allele- specific motifs revealed by sequencingof self- peptides eluted from MHC molecules Sendai NP 321-332 APGNYPAL951 Falk et al., Allele- virus specific motifs revealed by sequencing ofself- peptides eluted from MHC molecules VPYGSFKHV 952 Morel et al.,Processing of some antigens by the standard proteasome but not by theimmunoproteasome results in poor presentation by dendritic cells,Immunity, vol. 12:107-117, 2000. MOTIFS influenza PRS NP K^(d) TYQRTRALV953 5,747,269    restricted peptide motif self peptide P815 K^(d)SYFPEITHI 954 ″ restricted peptide motif influenza JAP HA K^(d)IYATVAGSL 955 ″ restricted peptide motif influenza JAP HA K^(d)VYQILAIYA 956 ″ restricted peptide motif influenza PR8 HA K^(d)IYSTVASSL 957 ″ restricted peptide motif influenza JAP HA K^(d)LYQNVGTYV 958 ″ restricted peptide motif HLA-A24 RYLENGKETL 959 ″HLA-Cw3 RYLKNGKETL 960 ″ P815 tumour ″ KYQAVTTTL 961 ″ antigenPlasmodium CSP ″ SYIPSAEKI 962 ″ berghei Plasmodium CSP ″ SYVPSAEQI 963″ yoelii influenza NP D^(b) - ASNENMETM 964 ″ restricted peptide motifadenovirus EIA D^(b) - SGPSNTPPEI 965 ″ restricted peptide motiflymphocytic D^(b) - SGVENPGGYC 966 ″ chorio- restricted L meningitispeptide motif simian virus 40 T D^(b) - SAINNY... 967 ″ restrictedpeptide motif HIV reverse HLA-A2.1 - ILKEPVHGV 968 ″ transcriptaserestricted peptide motif influenza HLA-A2.1 - GILGFVFTL 969 ″ matrixrestricted protein peptide motif influenza influenza HLA-A2.1 -ILGFVFTLTV 970 ″ matrix restricted protein peptide motif HIV Gag proteinFLQSRPEPT 971 ″ HIV Gag protein AMQMLKE.. 972 ″ HIV Gag proteinPIAPGQMRE 973 ″ HIV Gag protein QMKDCTERQ 974 ″ HLA- VYGVIQK 975 ″A*0205 - restricted peptide motif

[0134] TABLE 8 VSV-NP peptide (49-62) LCMV-NP peptide (118-132) LCMVglycoprotein peptide. 33-41

[0135] Still further embodiments are directed to methods, uses,therapies and compositions related to epitopes with specificity for MHC,including, for example, those listed in Tables 9-13. Other embodimentsinclude one or more of the MHCs listed in Tables 9-13, includingcombinations of the same, while other embodiments specifically excludeany one or more of the MHCs or combinations thereof. Tables 11-13include frequencies for the listed HLA antigens. TABLE 9 Class I MHCMolecules Class I Human HLA-A1 HLA-A*0101 HLA-A*0201 HLA-A*0202HLA-A*0203 HLA-A*0204 HLA-A*0205 HLA-A*0206 HLA-A*0207 HLA-A*0209HLA-A*0214 HLA-A3 HLA-A*0301 HLA-A*1101 HLA-A23 HLA-A24 HLA-A25HLA-A*2902 HLA-A*3101 HLA-A*3302 HLA-A*6801 HLA-A*6901 HLA-B7 HLA-B*0702HLA-B*0703 HLA-B*0704 HLA-B*0705 HLA-B8 HLA-B13 HLA-B14 HLA-B*1501 (B62)HLA-B17 HLA-B18 HLA-B22 HLA-B27 HLA-B*2702 HLA-B*2704 HLA-B*2705HLA-B*2709 HLA-B35 HLA-B*3501 HLA-B*3502 HLA-B*3701 HLA-B*3801HLA-B*39011 HLA-B*3902 HLA-B40 HLA-B*40012 (B60) HLA-B*4006 (B61)HLA-B44 HLA-B*4402 HLA-B*4403 HLA-B*4501 HLA-B*4601 HLA-B51 HLA-B*5101HLA-B*5102 HLA-B*5103 HLA-B*5201 HLA-B*5301 HLA-B*5401 HLA-B*5501HLA-B*5502 HLA-B*5601 HLA-B*5801 HLA-B*6701 HLA-B*7301 HLA-B*7801HLA-Cw*0102 HLA-Cw*0301 HLA-Cw*0304 HLA-Cw*0401 HLA-Cw*0601 HLA-Cw*0602HLA-Cw*0702 HLA-Cw8 HLA-Cw*1601 M HLA-G Murine H2-K^(d) H2-D^(d)H2-L^(d) H2-K^(b) H2-D^(b) H2-K^(k) H2-K^(kml) Qa-1^(a) Qa-2 H2-M3 RatRT1.A^(a) RT1.A^(l) Bovine Bota-A11 Bota-A20 Chicken B-F4 B-F12 B-F15B-F19 Chimpanzee Patr-A*04 Patr-A*11 Patr-B*01 Patr-B*13 Patr-B*16Baboon Papa-A*06 Macaque Mamu-A*01 Swine SLA (haplotype d/d) Virushomolog hCMV class I homolog UL18

[0136] TABLE 10 Class I MHC Molecules Class I Human HLA-A1 HLA-A*0101HLA-A*0201 HLA-A*0202 HLA-A*0204 HLA-A*0205 HLA-A*0206 HLA-A*0207HLA-A*0214 HLA-A3 HLA-A*1101 HLA-A24 HLA-A*2902 HLA-A*3101 HLA-A*3302HLA-A*6801 HLA-A*6901 HLA-B7 HLA-B*0702 HLA-B*0703 HLA-B*0704 HLA-B*0705HLA-B8 HLA-B14 HLA-B*1501 (B62) HLA-B27 HLA-B*2702 HLA-B*2705 HLA-B35HLA-B*3501 HLA-B*3502 HLA-B*3701 HLA-B*3801 HLA-B*39011 HLA-B*3902HLA-B40 HLA-B*40012 (B60) HLA-B*4006 (B61) HLA-B44 HLA-B*4402 HLA-B*4403HLA-B*4601 HLA-B51 HLA-B*5101 HLA-B*5102 HLA-B*5103 HLA-B*5201HLA-B*5301 HLA-B*5401 HLA-B*5501 HLA-B*5502 HLA-B*5601 HLA-B*5801HLA-B*6701 HLA-B*7301 HLA-B*7801 HLA-Cw*0102 HLA-Cw*0301 HLA-Cw*0304HLA-Cw*0401 HLA-Cw*0601 HLA-Cw*0602 HLA-Cw*0702 HLA-G Murine H2-K^(d)H2-D^(d) H2-L^(d) H2-K^(b) H2-D^(b) H2-K^(k) H2-K^(kml) Qa-2 RatRT1.A^(a) RT1.A^(l) Bovine Bota-A11 Bota-A20 Chicken B-F4 B-F12 B-F15B-F19 Virus homolog hCMV class I homolog UL18

[0137] TABLE 11 Estimated gene frequencies of HLA-A antigens CAU AFR ASILAT NAT Antigen Gf^(a) SE^(b) Gf SE Gf SE Gf SE Gf SE A1 15.1843 0.04895.7256 0.0771 4.4818 0.0846 7.4007 0.0978 12.0316 0.2533 A2 28.65350.0619 18.8849 0.1317 24.6352 0.1794 28.1198 0.1700 29.3408 0.3585 A313.3890 0.0463 8.4406 0.0925 2.6454 0.0655 8.0789 0.1019 11.0293 0.2437A28 4.4652 0.0280 9.9269 0.0997 1.7657 0.0537 8.9446 0.1067 5.38560.1750 A36 0.0221 0.0020 1.8836 0.0448 0.0148 0.0049 0.1584 0.01480.1545 0.0303 A23 1.8287 0.0181 10.2086 0.1010 0.3256 0.0231 2.92690.0628 1.9903 0.1080 A24 9.3251 0.0395 2.9668 0.0560 22.0391 0.172213.2610 0.1271 12.6613 0.2590 A9 unsplit 0.0809 0.0038 0.0367 0.00630.0858 0.0119 0.0537 0.0086 0.0356 0.0145 A9 total 11.2347 0.042913.2121 0.1128 22.4505 0.1733 16.2416 0.1382 14.6872 0.2756 A25 2.11570.0195 0.4329 0.0216 0.0990 0.0128 1.1937 0.0404 1.4520 0.0924 A263.8795 0.0262 2.8284 0.0547 4.6628 0.0862 3.2612 0.0662 2.4292 0.1191A34 0.1508 0.0052 3.5228 0.0610 1.3529 0.0470 0.4928 0.0260 0.31500.0432 A43 0.0018 0.0006 0.0334 0.0060 0.0231 0.0062 0.0055 0.00280.0059 0.0059 A66 0.0173 0.0018 0.2233 0.0155 0.0478 0.0089 0.03990.0074 0.0534 0.0178 A10 unsplit 0.0790 0.0038 0.0939 0.0101 0.12550.0144 0.0647 0.0094 0.0298 0.0133 A10 total 6.2441 0.0328 7.1348 0.08506.3111 0.0993 5.0578 0.0816 4.2853 0.1565 A29 3.5796 0.0252 3.20710.0582 1.1233 0.0429 4.5156 0.0774 3.4345 0.1410 A30 2.5067 0.021213.0969 0.1129 2.2025 0.0598 4.4873 0.0772 2.5314 0.1215 A31 2.73860.0221 1.6556 0.0420 3.6005 0.0761 4.8328 0.0800 6.0881 0.1855 A323.6956 0.0256 1.5384 0.0405 1.0331 0.0411 2.7064 0.0604 2.5521 0.1220A33 1.2080 0.0148 6.5607 0.0822 9.2701 0.1191 2.6593 0.0599 1.07540.0796 A74 0.0277 0.0022 1.9949 0.0461 0.0561 0.0096 0.2027 0.01670.1068 0.0252 A19 unsplit 0.0567 0.0032 0.2057 0.0149 0.0990 0.01280.1211 0.0129 0.0475 0.0168 A19 total 13.8129 0.0468 28.2593 0.150417.3846 0.1555 19.5252 0.1481 15.8358 0.2832 AX 0.8204 0.0297 4.95060.0963 2.9916 0.1177 1.6332 0.0878 1.8454 0.1925

[0138] TABLE 12 Estimated gene frequencies for HLA-B antigens CAU AFRASI LAT NAT Antigen Gf^(a) SE^(b) Gf SE Gf SE Gf SE Gf SE B7 12.17820.0445 10.5960 0.1024 4.2691 0.0827 6.4477 0.0918 10.9845 0.2432 B89.4077 0.0397 3.8315 0.0634 1.3322 0.0467 3.8225 0.0715  8.5789 0.2176B13 2.3061 0.0203 0.8103 0.0295 4.9222 0.0886 1.2699 0.0416  1.74950.1013 B14 4.3481 0.0277 3.0331 0.0566 0.5004 0.0287 5.4166 0.0846 2.9823 0.1316 B18 4.7980 0.0290 3.2057 0.0582 1.1246 0.0429 4.23490.0752  3.3422 0.1391 B27 4.3831 0.0278 1.2918 0.0372 2.2355 0.06032.3724 0.0567  5.1970 0.1721 B35 9.6614 0.0402 8.5172 0.0927 8.12030.1122 14.6516 0.1329 10.1198 0.2345 B37 1.4032 0.0159 0.5916 0.02521.2327 0.0449 0.7807 0.0327  0.9755 0.0759 B41 0.9211 0.0129 0.81830.0296 0.1303 0.0147 1.2818 0.0418  0.4766 0.0531 B42 0.0608 0.00335.6991 0.0768 0.0841 0.0118 0.5866 0.0284  0.2856 0.0411 B46 0.00990.0013 0.0151 0.0040 4.9292 0.0886 0.0234 0.0057  0.0238 0.0119 B470.2069 0.0061 0.1305 0.0119 0.0956 0.0126 0.1832 0.0159  0.2139 0.0356B48 0.0865 0.0040 0.1316 0.0119 2.0276 0.0575 1.5915 0.0466  1.02670.0778 B53 0.4620 0.0092 10.9529 0.1039 0.4315 0.0266 1.6982 0.0481 1.0804 0.0798 B59 0.0020 0.0006 0.0032 0.0019 0.4277 0.0265 0.00550.0028  0^(c) — B67 0.0040 0.0009 0.0086 0.0030 0.2276 0.0194 0.00550.0028  0.0059 0.0059 B70 0.3270 0.0077 7.3571 0.0866 0.8901 0.03821.9266 0.0512  0.6901 0.0639 B73 0.0108 0.0014 0.0032 0.0019 0.01320.0047 0.0261 0.0060  0^(c) — B51 5.4215 0.0307 2.5980 0.0525 7.47510.1080 6.8147 0.0943  6.9077 0.1968 B52 0.9658 0.0132 1.3712 0.03833.5121 0.0752 2.2447 0.0552  0.6960 0.0641 B5 unsplit 0.1565 0.00530.1522 0.0128 0.1288 0.0146 0.1546 0.0146  0.1307 0.0278 B5 total 6.54380.0435 4.1214 0.0747 11.1160 0.1504 9.2141 0.1324  7.7344 0.2784 B4413.4838 0.0465 7.0137 0.0847 5.6807 0.0948 9.9253 0.1121 11.8024 0.2511B45 0.5771 0.0102 4.8069 0.0708 0.1816 0.0173 1.8812 0.0506  0.76030.0670 B12 unsplit 0.0788 0.0038 0.0280 0.0055 0.0049 0.0029 0.01930.0051  0.0654 0.0197 B12 total 14.1440 0.0474 11.8486 0.1072 5.86730.0963 11.8258 0.1210 12.6281 0.2584 B62 5.9117 0.0320 1.5267 0.04049.2249 0.1190 4.1825 0.0747  6.9421 0.1973 B63 0.4302 0.0088 1.88650.0448 0.4438 0.0270 0.8083 0.0333  0.3738 0.0471 B75 0.0104 0.00140.0226 0.0049 1.9673 0.0566 0.1101 0.0123  0.0356 0.0145 B76 0.00260.0007 0.0065 0.0026 0.0874 0.0120 0.0055 0.0028  0 — B77 0.0057 0.00100.0119 0.0036 0.0577 0.0098 0.0083 0.0034  0^(c) 0.0059 B15 unsplit0.1305 0.0049 0.0691 0.0086 0.4301 0.0266 0.1820 0.0158  0.0059 0.0206B15 total 6.4910 0.0334 3.5232 0.0608 12.2112 0.1344 5.2967 0.0835 0.0715 0.2035  7.4290 B38 2.4413 0.0209 0.3323 0.0189 3.2818 0.07281.9652 0.0517  1.1017 0.0806 B39 1.9614 0.0188 1.2893 0.0371 2.03520.0576 6.3040 0.0909  4.5527 0.1615 B16 unsplit 0.0638 0.0034 0.02370.0051 0.0644 0.0103 0.1226 0.0130  0.0593 0.0188 B16 total 4.46670.0280 1.6453 0.0419 5.3814 0.0921 8.3917 0.1036  5.7137 0.1797 B573.5955 0.0252 5.6746 0.0766 2.5782 0.0647 2.1800 0.0544  2.7265 0.1260B58 0.7152 0.0114 5.9546 0.0784 4.0189 0.0803 1.2481 0.0413  0.93980.0745 B17 unsplit 0.2845 0.0072 0.3248 0.0187 0.3751 0.0248 0.14460.0141  0.2674 0.0398 B17 total 4.5952 0.0284 11.9540 0.1076 6.97220.1041 3.5727 0.0691  3.9338 0.1503 B49 1.6452 0.0172 2.6286 0.05280.2440 0.0200 2.3353 0.0562  1.5462 0.0953 B50 1.0580 0.0138 0.86360.0304 0.4421 0.0270 1.8883 0.0507  0.7862 0.0681 B21 unsplit 0.07020.0036 0.0270 0.0054 0.0132 0.0047 0.0771 0.0103  0.0356 0.0145 B21total 2.7733 0.0222 3.5192 0.0608 0.6993 0.0339 4.3007 0.0755  2.36800.1174 B54 0.0124 0.0015 0.0183 0.0044 2.6873 0.0660 0.0289 0.0063 0.0534 0.0178 B55 1.9046 0.0185 0.4895 0.0229 2.2444 0.0604 0.95150.0361  1.4054 0.0909 B56 0.5527 0.0100 0.2686 0.0170 0.8260 0.03680.3596 0.0222  0.3387 0.0448 B22 unsplit 0.1682 0.0055 0.0496 0.00730.2730 0.0212 0.0372 0.0071  0.1246 0.0272 B22 total 2.0852 0.02170.8261 0.0297 6.0307 0.0971 1.3771 0.0433  1.9221 0.1060 B60 5.22220.0302 1.5299 0.0404 8.3254 0.1135 2.2538 0.0553  5.7218 0.1801 B611.1916 0.0147 0.4709 0.0225 6.2072 0.0989 4.6691 0.0788  2.6023 0.1231B40 unsplit 0.2696 0.0070 0.0388 0.0065 0.3205 0.0230 0.2473 0.0184 0.2271 0.0367 B40 total 6.6834 0.0338 2.0396 0.0465 14.8531 0.14627.1702 0.0963  8.5512 0.2168 BX 1.0922 0.0252 3.5258 0.0802 3.87490.0988 2.5266 0.0807  1.9867 0.1634

[0139] TABLE 13 Estimated gene frequencies of HLA-DR antigens CAU AFRASI LAT NAT Antigen Gf^(a) SE^(b) Gf SE Gf SE Gf SE Gf SE DR1 10.22790.0413 6.8200 0.0832 3.4628 0.0747 7.9859 0.1013 8.2512 0.2139 DR215.2408 0.0491 16.2373 0.1222 18.6162 0.1608 11.2389 0.1182 15.39320.2818 DR3 10.8708 0.0424 13.3080 0.1124 4.7223 0.0867 7.8998 0.100810.2549 0.2361 DR4 16.7589 0.0511 5.7084 0.0765 15.4623 0.1490 20.53730.1520 19.8264 0.3123 DR6 14.3937 0.0479 18.6117 0.1291 13.4471 0.140417.0265 0.1411 14.8021 0.2772 DR7 13.2807 0.0463 10.1317 0.0997 6.92700.1040 10.6726 0.1155 10.4219 0.2378 DR8 2.8820 0.0227 6.2673 0.08006.5413 0.1013 9.7731 0.1110 6.0059 0.1844 DR9 1.0616 0.0139 2.96460.0559 9.7527 0.1218 1.0712 0.0383 2.8662 0.1291 DR10 1.4790 0.01632.0397 0.0465 2.2304 0.0602 1.8044 0.0495 1.0896 0.0801 DR11 9.31800.0396 10.6151 0.1018 4.7375 0.0869 7.0411 0.0955 5.3152 0.1740 DR121.9070 0.0185 4.1152 0.0655 10.1365 0.1239 1.7244 0.0484 2.0132 0.1086DR5 unsplit 1.2199 0.0149 2.2957 0.0493 1.4118 0.0480 1.8225 0.04981.6769 0.0992 DR5 total 12.4449 0.0045 17.0260 0.1243 16.2858 0.151610.5880 0.1148 9.0052 0.2218 DRX 1.3598 0.0342 0.8853 0.0760 2.55210.1089 1.4023 0.0930 2.0834 0.2037

[0140] It can be desirable to express housekeeping peptides in thecontext of a larger protein. Processing can be detected even when asmall number of amino acids are present beyond the terminus of anepitope. Small peptide hormones are usually proteolytically processedfrom longer translation products, often in the size range ofapproximately 60-120 amino acids. This fact has led some to assume thatthis is the minimum size that can be efficiently translated. In someembodiments, the housekeeping peptide can be embedded in a translationproduct of at least about 60 amino acids, in others 70, 80, 90 aminoacids, and in still others 100, 110 or 120 amino acids, for example. Inother embodiments the housekeeping peptide can be embedded in atranslation product of at least about 50, 30, or 15 amino acids.

[0141] Due to differential proteasomal processing, the immunoproteasomeof the pAPC produces peptides that are different from those produced bythe housekeeping proteasome in peripheral body cells. Thus, inexpressing a housekeeping peptide in the context of a larger protein, itis preferably expressed in the pAPC in a context other than itsfull-length native sequence, because, as a housekeeping epitope, it isgenerally only efficiently processed from the native protein by thehousekeeping proteasome, which is not active in the pAPC. In order toencode the housekeeping epitope in a DNA sequence encoding a largerpolypeptide, it is useful to find flanking areas on either side of thesequence encoding the epitope that permit appropriate cleavage by theimmunoproteasome in order to liberate that housekeeping epitope. Such asequence promoting appropriate processing is referred to hereinafter ashaving substrate or liberation sequence function. Altering flankingamino acid residues at the N-terminus and C-terminus of the desiredhousekeeping epitope can facilitate appropriate cleavage and generationof the housekeeping epitope in the pAPC. Sequences embeddinghousekeeping epitopes can be designed de novo and screened to determinewhich can be successfully processed by immunoproteasomes to liberatehousekeeping epitopes.

[0142] Alternatively, another strategy is very effective for identifyingsequences allowing production of housekeeping epitopes in APC. Acontiguous sequence of amino acids can be generated from head to tailarrangement of one or more housekeeping epitopes. A construct expressingthis sequence is used to immunize an animal, and the resulting T cellresponse is evaluated to determine its specificity to one or more of theepitopes in the array. These immune responses indicate housekeepingepitopes that are processed in the pAPC effectively. The necessaryflanking areas around this epitope are thereby defined. The use offlanking regions of about 4-6 amino acids on either side of the desiredpeptide can provide the necessary information to facilitate proteasomeprocessing of the housekeeping epitope by the immunoproteasome.Therefore, a substrate or liberation sequence of approximately 16-22amino acids can be inserted into, or fused to, any protein sequenceeffectively to result in that housekeeping epitope being produced in anAPC. In some embodiments, a broader context of a substrate sequence canalso influence processing. In such embodiments, comparisons of aliberaton sequence in a variety of contexts can be useful in furtheroptimizing a particular substrate sequence. In alternate embodiments thewhole head-to-tail array of epitopes, or just the epitopes immediatelyadjacent to the correctly processed housekeeping epitope can besimilarly transferred from a test construct to a vaccine vector.

[0143] In a preferred embodiment, the housekeeping epitopes can beembedded between known immune epitopes, or segments of such, therebyproviding an appropriate context for processing. The abutment ofhousekeeping and immune epitopes can generate the necessary context toenable the immunoproteasome to liberate the housekeeping epitope, or alarger fragment, preferably including a correct C-terminus. It can beuseful to screen constructs to verify that the desired epitope isproduced. The abutment of housekeeping epitopes can generate a sitecleavable by the immunoproteasome. Some embodiments of the inventionemploy known epitopes to flank housekeeping epitopes in test substrates;in others, screening as described below is used, whether the flankingregions are arbitrary sequences or mutants of the natural flankingsequence, and whether or not knowledge of proteasomal cleavagepreferences are used in designing the substrates.

[0144] Cleavage at the mature N-terminus of the epitope, whileadvantageous, is not required, since a variety of N-terminal trimmingactivities exist in the cell that can generate the mature N-terminus ofthe epitope subsequent to proteasomal processing. It is preferred thatsuch N-terminal extension be less than about 25 amino acids in lengthand it is further preferred that the extension have few or no prolineresidues. Preferably, in screening, consideration is given not only tocleavage at the ends of the epitope (or at least at its C-terminus), butconsideration also can be given to ensure limited cleavage within theepitope.

[0145] Shotgun approaches can be used in designing test substrates andcan increase the efficiency of screening. In one embodiment multipleepitopes can be assembled one after the other, with individual epitopespossibly appearing more than once. The substrate can be screened todetermine which epitopes can be produced. In the case where a particularepitope is of concern, a substrate can be designed in which it appearsin multiple different contexts. When a single epitope appearing in morethan one context is liberated from the substrate additional secondarytest substrates, in which individual instances of the epitope areremoved, disabled, or are unique, can be used to determine which arebeing liberated and truly confer substrate or liberation sequencefunction.

[0146] Several readily practicable screens exist. A preferred in vitroscreen utilizes proteasomal digestion analysis, using purifiedimmunoproteasomes, to determine if the desired housekeeping epitope canbe liberated from a synthetic peptide embodying the sequence inquestion. The position of the cleavages obtained can be determined bytechniques such as mass spectrometry, HPLC, and N-terminal poolsequencing; as described in greater detail in U.S. patent applicationSer. Nos. 09/561,074, 09/560,465 and 10/117,937, and Provisional U.S.Patent Application Nos. 60/282,211, 60/337,017, and 60/363, 210, whichwere all cited and incorporated by reference above.

[0147] Alternatively, in vivo and cell-based screens such asimmunization or target sensitization can be employed. For immunization anucleic acid construct capable of expressing the sequence in question isused. Harvested CTL can be tested for their ability to recognize targetcells presenting the housekeeping epitope in question. Such targetscells are most readily obtained by pulsing cells expressing theappropriate MHC molecule with synthetic peptide embodying the maturehousekeeping epitope. Alternatively, immunization can be carried outusing cells known to express housekeeping proteasome and the antigenfrom which the housekeeping epitope is derived, either endogenously orthrough genetic engineering. To use target sensitization as a screen,CTL, or preferably a CTL clone, that recognizes the housekeeping epitopecan be used. In this case it is the target cell that expresses theembedded housekeeping epitope (instead of the pAPC during immunization)and it must express immunoproteasome. Generally, the cell or target cellcan be transformed with an appropriate nucleic acid construct to conferexpression of the embedded housekeeping epitope. Loading with asynthetic peptide embodying the embedded epitope using peptide loadedliposomes, or complexed with cationic lipid protein transfer reagentssuch as BIOPORTER™ (Gene Therapy Systems, San Diego, Calif.), representsan alternative.

[0148] Once sequences with substrate or liberation sequence function areidentified they can be encoded in nucleic acid vectors, chemicallysynthesized, or produced recombinantly. In any of these forms they canbe incorporated into immunogenic compositions. Such compositions can beused in vitro in vaccine development or in the generation or expansionof CTL to be used in adoptive immunotherapy. In vivo they can be used toinduce, amplify or sustain and active immune response. The uptake ofpolypeptides for processing and presentation can be greatly enhanced bypackaging with cationic lipid, the addition of a tract of cationic aminoacids such as poly-L-lysine (Ryser, H. J. et al., J. Cell Physiol.113:167-178, 1982; Shen, W. C. & Ryser, H. J., Proc. Natl. Aced. Sci.USA 75:1872-1876, 1978), the incorporation into branched structures withimportation signals (Sheldon, K. et al., Proc. Natl. Aced. Sci. USA92:2056-2060, 1995), or mixture with or fusion to polypeptides withprotein transfer function including peptide carriers such as pep-1(Morris, M. C., et al., Nat. Biotech. 19:1173-1176, 2001), the PreS2translocation motif of hepatitis B virus surface antigen, VP22 of herpesviruses, and HIV-TAT protein (Oess, S. & Hildt, E., Gene Ther.7:750-758, 2000; Ford, K. G., et al., Gene Ther. 8:1-4, 2001; Hung, C.F. et al., J. Virol. 76:2676-2682, 2002; Oliveira, S. C., et al. Hum.Gene Ther. 12:1353-1359, 2001; Normand, N. et al., J. Biol. Chem.276:15042-15050, 2001; Schwartz, J. J. & Zhang, S., Curr. Opin. Mol.Ther. 2:162-167, 2000; Elliot G., 7 Hare, P. Cell 88:223-233, 1997),among other methodologies. Particularly for fusion proteins theimmunogen can be produced in culture and the purified proteinadministered or, in the alternative, the nucleic acid vector can beadministered so that the immunogen is produced and secreted by cellstransformed in vivo. In either scenario the transport function of thefusion protein facilitates uptake by pAPC.

[0149] The following examples are intended for illustration purposesonly, and should not be construed as limiting the scope of the inventionin any way.

EXAMPLES Example 1

[0150] A recombinant DNA plasmid vaccine, pMA2M, which encodes onepolypeptide with an HLA A2-specific CTL epitope ELAGIGILTV (SEQ IDNO. 1) from melan-A (26-35A27L), and a portion (amino acids 31-96) ofmelan-A (SEQ ID NO. 2) including the epitope clusters at amino acids31-48 and 56-69, was constructed. These clusters were previouslydisclosed in U.S. patent application Ser. No. 09/561,571 entitledEPITOPE CLUSTERS incorporated by reference above. Flanking the definedmelan-A CTL epitope are short amino acid sequences derived from humantyrosinase (SEQ ID NO. 3) to facilitate liberation of the melan-Ahousekeeping epitope by processing by the immunoproteasome. In addition,these amino acid sequences represent potential CTL epitopes themselves.The cDNA sequence for the polypeptide in the plasmid is under thecontrol of promoter/enhancer sequence from cytomegalovirus (CMVp) (seeFIG. 4), which allows efficient transcription of messenger for thepolypeptide upon uptake by APCs. The bovine growth hormonepolyadenylation signal (BGH polyA) at the 3′ end of the encodingsequence provides a signal for polyadenylation of the messenger toincrease its stability as well as for translocation out of nucleus intothe cytoplasm for translation. To facilitate plasmid transport into thenucleus after uptake, a nuclear import sequence (NIS) from simian virus40 (SV40) has been inserted in the plasmid backbone. The plasmid carriestwo copies of a CpG immunostimulatory motif, one in the NIS sequence andone in the plasmid backbone. Lastly, two prokaryotic genetic elements inthe plasmid are responsible for amplification in E. coli, the kanamycinresistance gene (Kan R) and the pMB1 bacterial origin of replication.

[0151] Substrate or Liberation Sequence

[0152] The amino acid sequence of the encoded polypeptide (94 amino acidresidues in length) (SEQ ID NO. 4) containing a 28 amino acid substrateor liberation sequence at its N-terminus (SEQ ID NO. 5) is given below:MLLAVLYCL-ELAGIGILTV-YMDGTMSQV-GILTVILGVLLLIGCWYCRRRNGYRALMDKSLHVGTQCALTRRCPQEGFD HRDSKVSLQEKNCEPV

[0153] The first 9 amino acid residues are derived from tyrosinase₁₋₉(SEQ ID NO. 6), the next ten constitute melan-A (26-35A27L) (SEQ ID NO.1), and amino acid residues 20 to 29 are derived from tyrosinase₃₆₉₋₃₇₇(SEQ ID NO. 7). These two tyrosinase nonamer sequences both representpotential HLA A2-specific CTL epitopes. Amino acid residues 10-19constitute melan-A (26-35A27L) an analog of an HLA A2-specific CTLepitope from melan-A, EAAGIGILTV (SEQ ID NO. 8), with an elevatedpotency in inducing CTL responses during in vitro immunization of humanPBMC and in vivo immunization in mice. The segment of melan-Aconstituting the rest of the polypeptide (amino acid residues 30 to 94)contain a number of predicted HLA A2-specific epitopes, including theepitope clusters cited above, and thus can be useful in generating aresponse to immune epitopes as described at length in the patentapplications ‘Epitope Synchronization in Antigen Presenting Cells’ and‘Epitope Clusters’ cited and incorporated by reference above. Thisregion was also included to overcome any difficulties that can beassociated with the expression of shorter sequences. A drawing of pMA2Mis shown in FIG. 4.

[0154] Plasmid Construction

[0155] A pair of long complementary oligonucleotides was synthesizedwhich encoded the first 30 amino acid residues. In addition, uponannealing, these oligonucleotides generated the cohensive ends of Afl IIat the 5′ end and that of EcoR I at the 3′ end. The melan A₃₁₋₉₆ regionwas amplified with PCR using oligonucleotides carrying restriction sitesfor EcoR I at the 5′ end and Not I at the 3′ end. The PCR product wasdigested with EcoR I and Not I and ligated into the vector backbone,described in Example 1, that had been digested with Afl II and Not I,along with the annealed oligonucleotides encoding the amino terminalregion in a three-fragment ligation. The entire coding sequence wasverified by DNA sequencing. The sequence of the entire insert, from theAfl II site at the 5′ end to the Not I site at the 3′ end is disclosedas SEQ ID NO. 9. Nucleotides 12-293 encode the polypeptide.

Example 2

[0156] Three vectors containing melan-A (26-35A27L) (SEQ ID NO. 1) as anembedded housekeeping epitope were tested for their ability to induce aCTL response to this epitope in HLA-A2 transgenic HHD mice (Pascolo etal. J. Exp. Med. 185:2043-2051, 1997). One of the vectors was pMA2Mdescribed above (called pVAXM3 in FIG. 6). In pVAXM2 the same basicgroup of 3 epitopes was repeated several times with the flankingepitopes truncated by differing degrees in the various repeats of thearray. Specifically the cassette consisted of:M-Tyr(5-9)-ELA-Tyr(369-373)-Tyr(4-9)-ELA-Tyr(369-374)-Tyr(3-9)-ELA-Tyr(369-375)- Tyr(2-9)-ELA (SEQ ID NO. 10)

[0157] where ELA represents melan-A (26-35A27L) (SEQ ID NO. 1). Thiscassette was inserted in the same plasmid backbone as used for pVAXM3.The third, pVAXM1 is identical to pVAXM2 except that the epitope arrayis followed by an IRES (internal ribosome entry site forencephalomyocarditis virus) linked to a reading frame encoding melan-A31-70.

[0158] Four groups of three HHD A2.1 mice were injected intranodally insurgically exposed inguinal lymph nodes with 25 μl of 1 mg/ml plasmidDNA in PBS on days 0, 3, and 6, each group receiving one of the threevectors or PBS alone. On day 14 the spleens were harvested andrestimulated in vitro one time with 3-day LPS blasts pulsed with peptide(melan-A (26-35A27L) (SEQ ID NO. 1)). The in vitro cultures weresupplemented with Rat T-Stim (Collaborative Biomedical Products) on the3^(rd) day and assayed for cytolytic activity on the 7^(th) day using astandard ⁵¹Cr-release assay. FIGS. 5 to 8 show % specific lysis obtainedusing the cells immunized with PBS, pVAXM1, pVAXM2, and pVAXM3,respectively on T2 target cells and T2 target cells pulsed with melan-A(26-35A27L) (ELA) (SEQ ID NO. 1). All three vectors generated strong CTLresponses. These data indicated that the plasmids have been taken up byAPCs, the encoded polypeptide has been synthesized and proteolyticallyprocessed to produce the decamer epitope in question (that is, it hadsubstrate or liberation sequence function), and that the epitope becameHLA-A2 bound for presentation. Also, an isolated variant of pVAXM2, thatterminates after the 55^(th) amino acid, worked similarly well as thefull length version (data not shown). Whether other potential epitopeswithin the expression cassette can also be produced and be active ininducing CTL responses can be determined by testing for CTL activityagainst target cells pulsed with corresponding synthetic peptides.

Example 3

[0159] An NY-ESO-1 (SEQ ID NO. 11) Substrate/Liberation Sequence

[0160] Six other epitope arrays were tested leading to theidentification of a substrate/liberation sequence for the housekeepingepitope NY-ESO-1₁₅₇₋₁₆₅ (SEQ ID NO. 12). The component epitopes of thearrays were: SSX-2₄₁₋₄₉: KASEKIFYV (SEQ ID NO. 13) Array element ANY-ESO-1₁₅₇₋₁₆₅: SLLMWITQC (SEQ ID NO. 12) Array element BNY-ESO-1₁₆₃₋₁₇₁: TQCFLPVFL (SEQ ID NO. 14) Array element C PSMA₂₈₈₋₂₉₇:GLPSIPVHPI (SEQ ID NO. 15) Array element D TYR₄₋₉: AVLYCL (SEQ ID NO.16) Array element E

[0161] The six arrays had the following arrangements of elements afterstarting with an initiator methionine: pVAX-PC-A: B-A-D-D-A-B-A-ApVAX-PC-B: D-A-B-A-A-D-B-A pVAX-PC-C: E-A-D-B-A-B-E-A-A pVAX-BC-A:B-A-C-B-A-A-C-A pVAX-BC-B: C-A-B-C-A-A-B-A pVAX-BC-C: E-A-A-B-C-B-A-A

[0162] These arrays were inserted into the same vector backbonedescribed in the examples above. The plasmid vectors were used toimmunize mice essentially as described in Example 2 and the resultingCTL were tested for their ability to specifically lyse target cellspulsed with the peptide NY-ESO-1 157-165, corresponding to element Babove. Both pVAX-PC-A and pVAX-BC-A were found to induce specific lyticactivity. Comparing the contexts of the epitope (element B) in thevarious arrays, and particularly between pVAX-PC-A and pVAX-BC-A,between pVAX-PC-A and pVAX-PC-B, and between pVAX-BC-A and pVAX-BC-C, itwas concluded that it was the first occurrence of the epitope inpVAX-PC-A and pVAX-BC-A that was being correctly processed andpresented. In other words an initiator methionine followed by elementsB-A constitute a substrate/liberation sequence for the presentation ofelement B. On this basis a new expression cassette for use as a vaccinewas constructed encoding the following elements:

[0163] An initiator methionine,

[0164] NY-ESO-1₁₅₇₋₁₆₅ (bold)—a housekeeping epitope,

[0165] SSX2₄₁₋₄₉ (italic)—providing appropriate context for processing,and

[0166] NY-ESO-1₇₇₋₁₈₀—to avoid “short sequence” problems and provideimmune epitopes.

[0167] Thus the construct encodes the amino acid sequence:M-SLLMWITQC-KASEKIFYV-RCGARGPESRLLEFYLAMPFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNILTIRLTAADHRQLQLSISSCLQQLSLLMWITQCFLPVFLAQPPS GQRR (SEQ ID NO. 17)

[0168] and MSLLMWITQCKASEKIFYV (SEQ ID NO. 18) constitutes theliberation or substrate sequence. A polynucleotide encoding SEQ ID NO.17 (SEQ ID NO. 19: nucleotides 12-380) was inserted into the sameplasmid backbone as used for pMA2M generating the plasmid pN157.

Example 4

[0169] A construct similar to pN157 containing the whole epitope arrayfrom pVAX-PC-A was also made and designated pBPL. Thus the encoded aminoacid sequence in pBPL is: M-SLLMWITQC-KASEKIFYV-GLPSIPVHPI-GLPSIPVHIPI-KASEKIFYV-SLLMWITQC-KASEKIFYV-KASEKIFYV-RCGARGPESRLLEFYLAMPFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNILTIRLTAADHRQLQLSISSCLQQLSLLMWITQCFLPVFLAQPPS GQRR. (SEQ ID NO. 20)

[0170] SEQ ID NO. 21 is the polynucleotide encoding SEQ ID NO. 20 usedin pBPL.

[0171] A portion of SEQ ID NO. 20, IKASEKIFYVSLLMWITQCKASEKIFYVK (SEQ IDNO. 22) was made as a synthetic peptide and subjected to in vitroproteasomal digestion analysis with human immunoproteasome, utilizingboth mass spectrometry and N-terminal pool sequencing. Theidentification of a cleavage after the C residue indicates that thissegment of the construct can function as a substrate or liberationsequence for NY-ESO-1₁₅₇₋₁₆₅ (SEQ ID NO. 12) epitope (see FIG. 9). FIG.10 shows the differential processing of the SLLMWITQC epitope (SEQ IDNO. 12) in its native context where the cleavage following the C is moreefficiently produced by housekeeping than immunoproteasome. Theimmunoproteasome also produces a major cleavage internal to the epitope,between the T and the Q when the epitope is in its native context, butnot in the context of SEQ ID NO. 22 (compare FIGS. 6 and 7).

Example 5

[0172] Screening of further epitope arrays led to the identification ofconstructs promoting the expression of the epitope SSX-2₄₁₋₄₉ (SEQ IDNO. 13). In addition to some of the array elements defined in Example 3,the following additional elements were also used: SSX-4₅₇₋₆₅: VMTKLGFKV(SEQ ID NO. 23) Array element F. PSMA₇₃₀₋₇₃₉: RQIYVAAFTV (SEQ ID NO. 24)Array element G.

[0173] A construct, denoted CTLA02, encoding an initiator methionine andthe array F-A-G-D-C-F-G-A, was found to successfully immunize HLA-A2transgenic mice to generate a CTL response recognizing the peptideSSX-2₄₁₋₄₉ (SEQ ID NO. 13).

[0174] As described above, it can be desirable to combine a sequencewith substrate or liberation sequence function with one that can beprocessed into immune epitopes. Thus SSX-2₁₅₋₁₈₃ (SEQ ID NO. 25) wascombined with all or part of the array as follows: CTLS1:F-A-G-D-C-F-G-A-SSX-2₁₅₋₁₈₃ (SEQ ID NO. 26) CTLS2:SSX-2₁₅₋₁₈₃-F-A-G-D-C-F-G-A (SEQ ID NO. 27) CTLS3: F-A-G-D-SSX-2₁₅₋₁₈₃(SEQ ID NO. 28) CTLS4: SSX-2₁₅₋₁₈₃-C-F-G-A. (SEQ ID NO. 29)

[0175] All of the constructs except CTLS3 were able to induce CTLrecognizing the peptide SSX-2₄₁₋₄₉ (SEQ ID NO. 13). CTLS3 was the onlyone of these four constructs which did not include the second element Afrom CTLA02 suggesting that it was this second occurrence of the elementthat provided substrate or liberation sequence function. In CTLS2 andCTLS4 the A element is at the C-terminal end of the array, as in CTLA02.In CTLS1 the A element is immediately followed by the SSX-2₁₅₋₁₈₃segment which begins with an alanine, a residue often found afterproteasomal cleavage sites (Toes, R. E. M., et al., J. Exp. Med.194:1-12, 2001). SEQ ID NO. 30 is the polynucleotide sequence encodingSEQ ID NO. 26 used in CTLS1, also called pCBP.

[0176] A portion of CTLS1 (SEQ ID NO. 26), encompassing array elementsF-A-SSX-2₁₅₋₂₃ with the sequence RQIYVAAFTV-KASEKIFYV-AQIPEKIQK (SEQ IDNO. 31), was made as a synthetic peptide and subjected to in vitroproteasomal digestion analysis with human immunoproteasome, utilizingboth mass spectrometry and N-terminal pool sequencing. The observationthat the C-terminus of the SSX-2₄₁₋₄₉ epitope (SEQ ID NO. 13) wasgenerated (see FIG. 11) provided further evidence in support ofsubstrate or liberation sequence function. The data in FIG. 12 showedthe differential processing of the SSX-2₄₁₋₄₉ epitope, KASEKIFYV (SEQ IDNO. 13), in its native context, where the cleavage following the V wasthe predominant cleavage produced by housekeeping proteasome, while theimmunoproteasome had several major cleavage sites elsewhere in thesequence. By moving this epitope into the context provided by SEQ ID NO.31 the desired cleavage became a major one and its relative frequencycompared to other immunoproteasome cleavages was increased (compareFIGS. 11 and 12). The data in FIG. 1B also showed the similarity inspecificity of mouse and human immunoproteasome lending support to theusefulness of the transgenic mouse model to predict human antigenprocessing.

Example 6

[0177] Screening also revealed substrate or liberation sequence functionfor a tyrosinase epitope, Tyr₂₀₇₋₂₁₅ (SEQ ID NO. 32), as part of anarray consisting of the sequence [Tyr₁₋₁₇-Tyr₂₀₇₋₂₁₅]₄,[MLLAVLYCLLWSFQTSA-FLPWHRLFL]₄, (SEQ ID NO. 33). The same vectorbackbone described above was used to express this array. This arraydiffers from those of the other examples in that the Tyr₁₋₁₇ segment,which was included as a source of immune epitopes, is used as a repeatedelement of the array. This is in contrast with the pattern shown in theother examples where sequence included as a source of immune epitopesand/or length occurred a single time at the beginning or end of thearray, the remainder of which was made up of individual epitopes orshorter sequences.

[0178] Plasmid Construction

[0179] The polynucleotide encoding SEQ ID NO. 33 was generated byassembly of annealed synthetic oligonucleotides. Four pairs ofcomplementary oligonucleotides were synthesized which span the entirecoding sequence with cohesive ends of the restriction sites of Afl IIand EcoR I at either terminus. Each complementary pair ofoligonucleotides were first annealed, the resultant DNA fragments wereligated stepwise, and the assembled DNA fragment was inserted into thesame vector backbone described above pre-digested with Afl II/EcoR I.The construct was called CTLT2/pMEL and SEQ ID NO. 34 is thepolynucleotide sequence used to encode SEQ ID NO. 33.

Example 7

[0180] Administration of a DNA Plasmid Formulation of aImmunotherapeutic for Melanoma to Humans.

[0181] An MA2M melanoma vaccine with a sequence as described in Example1 above, was formulated in 1% Benzyl alcohol, 1% ethyl alcohol, 0.5 mMEDTA, citrate-phosphate, pH 7.6. Aliquots of 200, 400, and 600 μg DNA/mlwere prepared for loading into MINIMED 407C infusion pumps. The catheterof a SILHOUETTE infusion set was placed into an inguinal lymph nodevisualized by ultrasound imaging. The pump and infusion set assembly wasoriginally designed for the delivery of insulin to diabetics. The usual17 mm catheter was substituted with a 31 mm catheter for thisapplication. The infusion set was kept patent for 4 days (approximately96 hours) with an infusion rate of about 25 μl/hour resulting in a totalinfused volume of approximately 2.4 ml. Thus the total administered doseper infusion was approximately 500, and 1000 μg; and can be 1500 μg,respectively, for the three concentrations described above. Following aninfusion, subjects were given a 10 day rest period before starting asubsequent infusion. Given the continued residency of plasmid DNA in thelymph node after administration and the usual kinetics of CTL responsefollowing disappearance of antigen, this schedule will be sufficient tomaintain the immunologic CTL response.

Example 8

[0182] SEQ ID NO. 22 is made as a synthetic peptide and packaged with acationic lipid protein transfer reagent. The composition is infuseddirectly into the inguinal lymph node (see example 7) at a rate of 200to 600 μg of peptide per day for seven days, followed by seven daysrest. An initial treatment of 3-8 cycles are conducted.

Example 9

[0183] A fusion protein is made by adding SEQ ID NO. 34 to the 3′ end ofa nucleotide sequence encoding herpes simplex virus 1 VP22 (SEQ ID NO.42) in an appropriate mammalian expression vector; the vector used aboveis suitable. The vector is used to transform HEK 293 cells and 48 to 72hours later the cells are pelleted, lysed and a soluble extractprepared. The fusion protein is purified by affinity chromatagraphyusing an anti-VP22 monoclonal antibody. The purified fusion protein isadministered intranodally at a rate of 10 to 100 μg per day for sevendays, followed by seven days rest. An initial treatment of 3-8 cyclesare conducted.

Examples 10-13

[0184] The following examples, Examples 10-13, all concern theprediction of 9-mer epitopes presented by HLA-A2.1, although theprocedure is equally applicable to any HLA type, or epitope length, forwhich a predictive algorithm or MHC binding assay is available.

Example 10 Melan-A/MART-1 (SEQ ID NO: 2)

[0185] This melanoma tumor-associated antigen (TuAA) is 118 amino acidsin length. Of the 110 possible 9-mers, 16 are given a score≧16 by theSYFPEITHI/Rammensee algorithm. (See Table 14). These represent 14.5% ofthe possible peptides and an average epitope density on the protein of0.136 per amino acid. Twelve of these overlap, covering amino acids22-49 of SEQ ID NO: 2 resulting in an epitope density for the cluster of0.428, giving a ratio, as described above, of 3.15. Another twopredicted epitopes overlap amino acids 56-69 of SEQ ID NO: 2, giving anepitope density for the cluster of 0.143, which is not appreciablydifferent than the average, with a ratio of just 1.05. See FIG. 1. TABLE14 SYFPEITHI (Rammensee algorithm) Results for Melan-A/MART-1 (SEQ IDNO: 2) Rank Start Score 1 31 27 2 56 26 3 35 26 4 32 25 5 27 25 6 29 247 34 23 8 61 20 9 33 19 10 22 19 11 99 18 12 36 18 13 28 18 14 87 17 1541 17 16 40 16

[0186] Restricting the analysis to the 9-mers predicted to have a halftime of dissociation of ≧5 minutes by the BIMAS-NIH/Parker algorithmleaves only 5. (See Table 15). The average density of epitopes in theprotein is now only 0.042 per amino acid. Three overlapping peptidescover amino acids 31-48 of SEQ ID NO: 2 and the other two cover 56-69 ofSEQ ID NO: 2, as before, giving ratios of 3.93 and 3.40, respectively.(See Table 16). TABLE 15 BIMAS-NIH/Parker algorithm Results forMelan-A/MART-1 (SEQ ID NO: 2) Rank Start Score Log(Score) 1 40 1289.013.11 2 56 1055.104 3.02 3 31 81.385 1.91 4 35 20.753 1.32 5 61 4.9680.70

[0187] TABLE 16 Predicted Epitope Clusters for Melan-A/MART-1 (SEQ IDNO: 2) Calculations(Epitopes/AAs) Cluster AA Peptides Cluster Wholeprotein Ratio 1 31-48 3, 4, 1 0.17 0.042 3.93 2 56-69 2, 5 0.14 0.0423.40

Example 11 SSX-2/HOM-MEL-40 (SEQ ID NO: 40)

[0188] This melanoma tumor-associated antigen (TuAA) is 188 amino acidsin length. Of the 180 possible 9-mers, 11 are given a score≧16 by theSYFPEITHI/Rammensee algorithm. These represent 6.1% of the possiblepeptides and an average epitope density on the protein of 0.059 peramino acid. Three of these overlap, covering amino acids 99-114 of SEQID NO: 40 resulting in an epitope density for the cluster of 0.188,giving a ratio, as described above, of 3.18. There are also overlappingpairs of predicted epitopes at amino acids 16-28, 57-57, and 167-183 ofSEQ ID NO: 40, giving ratios of 2.63, 3.11, and 2.01, respectively.There is an additional predicted epitope covering amino acids 5-28.Evaluating the region 5-28 of SEQ ID NO: 40 containing three epitopesgives an epitope density of 0.125 and a ratio 2.14.

[0189] Restricting the analysis to the 9-mers predicted to have a halftime of dissociation of ≧5 minutes by the BIMAS-NIH/Parker algorithmleaves only 6. The average density of epitopes in the protein is nowonly 0.032 per amino acid. Only a single pair overlap, at 167-180 of SEQID NO: 40, with a ratio of 4.48. However the top ranked peptide is closeto another single predicted epitope if that region, amino acids 41-65 ofSEQ ID NO: 40, is evaluated the ratio is 2.51, representing asubstantial difference from the average. See FIG. 2. TABLE 17SYFPEITHI/Rammensee algorithm for SSX-2/HOM-MEL-40 (SEQ ID NO: 40) RankStart Score 1 103 23 2 167 22 3 41 22 4 16 21 5 99 20 6 59 19 7 20 17 85 17 9 175 16 10 106 16 11 57 16

[0190] TABLE 18 Calculations(Epitopes/AAs) (SEQ ID NO: 40)Calculations(Epitopes/AAs) Cluster AA Peptides Cluster Whole proteinRatio 1  5 to 28 8, 4, 7 0.125 0.059 2.14 2 16-28 4, 7 0.15 0.059 2.63 357-67 11, 6 0.18 0.059 3.11 4  99-114 5, 1, 10 0.19 0.059 3.20 5 167-1832, 9 0.12 0.059 2.01

[0191] TABLE 19 BIMAS-NIH/Parker algorithm (SEQ ID NO: 40) Rank StartScore Log(Score) 1 41 1017.062 3.01 2 167 21.672 1.34 3 57 20.81 1.32 4103 10.433 1.02 5 172 10.068 1.00 6 16 6.442 0.81

[0192] TABLE 20 Calculations(Epitopes/AAs) (SEQ ID NO: 40) Cluster AAPeptides Cluster Whole protein Ratio 1 41-65 1, 3 0.08 0.032 2.51 2167-180 2, 5 0.14 0.032 4.48

Example 12 NY-ESO (SEQ ID NO: 11)

[0193] This tumor-associated antigen (TuAA) is 180 amino acids inlength. Of the 172 possible 9-mers, 25 are given a score≧16 by theSYFPEITHI/Rammensee algorithm. Like Melan-A above, these represent 14.5%of the possible peptides and an average epitope density on the proteinof 0.136 per amino acid. However the distribution is quite different.Nearly half the protein is empty with just one predicted epitope in thefirst 78 amino acids. Unlike Melan-A where there was a very tightcluster of highly overlapping peptides, in NY-ESO the overlaps aresmaller and extend over most of the rest of the protein. One set of 19overlapping peptides covers amino acids 108-174 of SEQ ID NO: 11,resulting in a ratio of 2.04. Another 5 predicted epitopes cover 79-104of SEQ ID NO: 11, for a ratio of just 1.38.

[0194] If instead one takes the approach of considering only the top 5%of predicted epitopes, in this case 9 peptides, one can examine whethergood clusters are being obscured by peptides predicted to be less likelyto bind to MHC. When just these predicted epitopes are considered we seethat the region 108-140 of SEQ ID NO: 11 contains 6 overlapping peptideswith a ratio of 3.64. There are also 2 nearby peptides in the region148-167 of SEQ ID NO: 11 with a ratio of 2.00. Thus the large cluster108-174 of SEQ ID NO: 11 can be broken into two smaller clusterscovering much of the same sequence.

[0195] Restricting the analysis to the 9-mers predicted to have a halftime of dissociation of ≧5 minutes by the BIMAS-NIH/Parker algorithmbrings 14 peptides into consideration. The average density of epitopesin the protein is now 0.078 per amino acid. A single set of 10overlapping peptides is observed, covering amino acids 144-171 of SEQ IDNO: 11, with a ratio of 4.59. All 14 peptides fall in the region 86-171of SEQ ID NO: 11 which is still 2.09 times the average density ofepitopes in the protein. While such a large cluster is larger than weconsider ideal it still offers a significant advantage over working withthe whole protein. See FIG. 3. TABLE 21 SYFPEITHI (Rammensee algorithm)Results for NY-ESO (SEQ ID NO: 11) Rank Start Score 1 108 25 2 148 24 3159 21 4 127 21 5 86 21 6 132 20 7 122 20 8 120 20 9 115 20 10 96 20 11113 19 12 91 19 13 166 18 14 161 18 15 157 18 16 151 18 17 137 18 18 7918 19 139 17 20 131 17 21 87 17 22 152 16 23 144 16 24 129 16 25 15 16

[0196] TABLE 22 Calculations(Epitopes/AAs) (SEQ ID NO: 11) Cluster AAPeptides Cluster Whole protein Ratio 1 108-140 1, 9, 8, 7, 4, 6 0.180.05 3.64 2 148-167 2, 3 0.10 0.05 2.00 3  79-104 5 12, 10, 18, 21 0.190.14 1.38 4 108-174 1, 11, 9, 8, 7, 4, 6, 17, 2, 16, 15, 3, 0.28 0.142.04 14, 13, 24, 20, 19, 23, 22

[0197] TABLE 23 BIMAS-NIH/Parker algorithm Results for NY-ESO (SEQ IDNO: 11) Rank Start Score Log(Score) 1 159 1197.321 3.08 2  86 429.5782.63 3 120 130.601 2.12 4 161 83.584 1.92 5 155 52.704 1.72 6 154 49.5091.69 7 157 42.278 1.63 8 108 21.362 1.33 9 132 19.425 1.29 10 145 13.6241.13 11 163 11.913 1.08 12 144 11.426 1.06 13 148 6.756 0.83 14 1524.968 0.70

[0198] TABLE 24 Calculations(Epitopes/AAs) (SEQ ID NO: 11) Cluster AAPeptides Cluster Whole protein Ratio 1  86-171 2, 8, 3, 9, 10, 12, 0.1630.078 2.09 13, 14, 6, 5, 7, 1, 4, 11 2 144-171 10, 12, 13, 14, 6, 0.360.078 4.59 5, 7, 1, 4, 11

Example 13 Tyrosinase (SEQ ID NO: 3)

[0199] This melanoma tumor-associated antigen (TuAA) is 529 amino acidsin length. Of the 521 possible 9-mers, 52 are given a score≧16 by theSYFPEITHI/Rammensee algorithm. These represent 10% of the possiblepeptides and an average epitope density on the protein of 0.098 peramino acid. There are 5 groups of overlapping peptides containing 2 to13 predicted epitopes each, with ratios ranging from 2.03 to 4.41,respectively. There are an additional 7 groups of overlapping peptides,containing 2 to 4 predicted epitopes each, with ratios ranging from 1.20to 1.85, respectively. The 17 peptides in the region 444-506 of SEQ IDNO: 3, including the 13 overlapping peptides above, constitutes acluster with a ratio of 2.20.

[0200] Restricting the analysis to the 9-mers predicted to have a halftime of dissociation of ≧5 minutes by the BIMAS-NIH/Parker algorithmbrings 28 peptides into consideration. The average density of epitopesin the protein under this condition is 0.053 per amino acid. At thisdensity any overlap represents more than twice the average density ofepitopes. There are 5 groups of overlapping peptides containing 2 to 7predicted epitopes each, with ratios ranging from 2.22 to 4.9,respectively. Only three of these clusters are common to the twoalgorithms. Several, but not all, of these clusters could be enlarged byevaluating a region containing them and nearby predicted epitopes. TABLE25 SYFPEITHI/Rammensee algorithm Results for Tyrosinase (SEQ ID NO: 3)Rank Start Score 1 490 34 2 491 31 3 487 28 4 1 27 5 2 25 6 482 23 7 38023 8 369 23 9 214 23 10 506 22 11 343 22 12 207 22 13 137 22 14 57 22 15169 20 16 118 20 17 9 20 18 488 19 19 483 19 20 480 19 21 479 19 22 47819 23 473 19 24 365 19 25 287 19 26 200 19 27 5 19 28 484 18 29 476 1830 463 18 31 444 18 32 425 18 33 316 18 34 187 18 35 402 17 36 388 17 37346 17 38 336 17 39 225 17 40 224 17 41 208 17 42 186 17 43 171 17 44514 16 45 494 16 46 406 16 47 385 16 48 349 16 49 184 16 50 167 16 51145 16 52 139 16

[0201] TABLE 26 Calculations(Epitopes/AAs) (SEQ ID NO: 3) Cluster AAPeptides Cluster Whole protein Ratio 1  1 to 17 4, 5, 27, 17 0.24 0.0982.39 2 137-153 13, 52, 51 0.18 0.098 1.80 3 167-179 15, 43, 50 0.230.098 2.35 4 184-195 34, 42, 49 0.25 0.098 2.54 5 200-222 26, 41, 9, 120.17 0.098 1.77 6 224-233 39, 40 0.20 0.098 2.03 7 336-357 38, 11, 37,48 0.18 0.098 1.85 8 365-377 24, 8 0.15 0.098 1.57 9 380-396 7, 47, 360.18 0.098 1.80 10 402-414 35, 46 0.15 0.098 1.57 11 473-502 29, 28, 23,22, 0.43 0.098 4.41 21, 20, 6, 19, 3, 18, 1, 2, 45 12 506-522 10, 440.12 0.098 1.20 444-522 31, 30, 23, 29, 0.22 0.098 2.20 22, 21, 20, 6,19, 28, 3, 18, 1, 2, 45, 10, 44

[0202] TABLE 27 BIMAS-NIH/Parker algorithm Results (SEQ ID NO: 3) RankStart Score Log(Score) 1 207 540.469 2.73 2 369 531.455 2.73 3 1 309.052.49 4 9 266.374 2.43 5 490 181.794 2.26 6 214 177.566 2.25 7 224143.451 2.16 8 171 93.656 1.97 9 506 87.586 1.94 10 487 83.527 1.92 11491 83.527 1.92 12 2 54.474 1.74 13 137 47.991 1.68 14 200 30.777 1.4915 208 26.248 1.42 16 460 21.919 1.34 17 478 19.425 1.29 18 365 17.141.23 19 380 16.228 1.21 20 444 13.218 1.12 21 473 13.04 1.12 22 5710.868 1.04 23 482 8.252 0.92 24 483 7.309 0.86 25 5 6.993 0.84 26 2255.858 0.77 27 343 5.195 0.72 28 514 5.179 0.71

[0203] TABLE 28 Calculations(Epitopes/AAs) (SEQ ID NO: 3) Cluster AAPeptides Cluster Whole protein Ratio 1  1 to 17 3, 12, 25, 4 0.24 0.0534.45 2 200-222 14, 1, 15, 6 0.17 0.053 3.29 3 224-233 7, 26 0.20 0.0533.78 4 365-377 18, 2 0.15 0.053 2.91 5 473-499 21, 17, 23, 24, 0.260.053 4.90 10, 5, 11 6 506-522 9, 28 0.12 0.053 2.22 7 365-388 18, 2, 190.13 0.053 2.36 8 444-499 20, 16, 21, 17, 0.16 0.053 3.03 23, 24, 10, 5,11 9 444-522 20, 16, 21, 17, 0.14 0.053 2.63 23, 24, 10, 5, 11, 9, 28 10200-233 14, 1, 15, 6, 0.18 0.053 3.33 7, 26

[0204] All references mentioned herein are hereby incorporated byreference in their entirety. Further, the present invention can utilizevarious aspects of the following, which are all incorporated byreference in their entirety: U.S. patent application Ser. No.09/380,534, filed on Sep. 1, 1999, entitled A METHOD OF INDUCING A CTLRESPONSE; Ser. No. 09/776,232, filed on Feb. 2, 2001, entitled METHOD OFINDUCING A CTL RESPONSE; Ser. No. 09/715,835, filed on Nov. 16, 2000,entitled AVOIDANCE OF UNDESIRABLE REPLICATION INTERMEDIATES IN PLASMIDPROPOGATION; Ser. No. 09/999,186, filed on Nov. 7, 2001, entitledMETHODS OF COMMERCIALIZING AN ANTIGEN; and Provisional U.S. PatentApplication No. 60/274,063, filed on Mar. 7, 2001, entitledANTI-NEOVASCULAR VACCINES FOR CANCER. TABLE 29 Partial listing of SEQ IDNOS.  1 ELAGIGILTV melan-A 26-35 (A27L)  2 Melan-A protein Accessionnumber: NP_005502  3 Tyrosinase protein Accession number: P14679  4MLLAVLYCLELAGIGILTVYMDGTMSQVGILTVILGVL pMA2M expressionLLIGCWYCRRRNGYRALMDKSLHVGTQCALTRRCPQEG product FDHRDSKVSLQEKNCEPV  5MLLAVLYCLELAGIGILTVYMDGTMSQV Liberation or substrate sequence for SEQ IDNO. 1 from pMA2M  6 MLLAVLYCL tyrosinase 1-9  7 YMDGTMSQV tyrosinase369-377  8 EAAGIGILTV melan-A 26-35  9cttaagccaccatgttactagctgttttgtactgcctg pMA2M insertgaactagcagggatcggcatattgacagtgtatatggatggaacaatgtcccaggtaggaattctgacagtgatcctgggagtcttactgctcatcggctgttggtattgtagaagacgaaatggatacagagccttgatggataaaagtcttcatgttggcactcaatgtgccttaacaagaagatgcccacaagaagggtttgatcatcgggacagcaaagtgtctcttcaagagaaaaactgtgaacctgtgtagtgagcggc cgc 10MVLYCLELAGIGILTVYMDGTAVLYCLELAGIGILTVY Epitope array fromMDGTMLAVLYCLELAGIGILTVYMDGTMSLLAVLYCLE pVAXM2 and pVAXM1 LAGIGILTV 11NY-ESO-1 protein Accession number: P78358 12 SLLMWITQC NY-ESO-1 157-16513 KASEKIFYV SSX-2 41-49 14 TQCFLPVFL NY-ESO-1 163-171 15 GLPSIPVHPIPSMA 288-297 16 AVLYCL tyrosinase 4-9 17MSLLMWITQCKASEKIFYVRCGARGPESRLLEFYLAMP pN157 expressionFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNIL productTIRLTAADHRQLQLSISSCLQQLSLLMWITQCFLPVFL AQPPSGQRR 18 MSLLMWITQCKASEKIFYVliberation or substrate sequence for SEQ ID NO. 12 from pN157 19cttaagccaccatgtccctgttgatgtggatcacgcag Insert for pN157tgcaaagcttcggagaaaatcttctacgtacggtgcggtgccagggggccggagagccgcctgcttgagttctacctcgccatgcctttcgcgacacccatggaagcagagctggcccgcaggagcctggcccaggatgccccaccgcttcccgtgccaggggtgcttctgaaggagttcactgtgtccggcaacatactgactatccgactgactgctgcagaccaccgccaactgcagctctccatcagctcctgtctccagcagctttccctgttgatgtggatcacgcagtgctttctgcccgtgtttttggctcagcctccctcagggcagaggcgc tagtgagaattc 20MSLLMWITQCKASEKIFYVGLPSIPVHPIGLPSIPVHP pBPL expressionIKASEKIFYVSLLMWITQCKASEKIFYVKASEKIFYVR productCGARGPESRLLEFYLAMPFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNILTIRLTAADHRQLQLSISSCL QQLSLLMWITQCFLPVFLAQPPSGQRR 21atgtccctgttgatgtggatcacgcagtgcaaagcttc pBPL insert codingggagaaaatcttctatgtgggtcttccaagtattcctg regionttcatccaattggtcttccaagtattcctgttcatccaattaaagcttcggagaaaatcttctatgtgtccctgttgatgtggatcacgcagtgcaaagcttcggagaaaatcttctatgtgaaagcttcggagaaaatcttctacgtacggtgcggtgccagggggccggagagccgcctgcttgagttctacctcgccatgcctttcgcgacacccatggaagcagagctggcccgcaggagcctggcccaggatgccccaccgcttcccgtgccaggggtgcttctgaaggagttcactgtgtccggcaacatactgactatccgactgactgctgcagaccaccgccaactgcagctctccatcagctcctgtctccagcagctttccctgttgatgtggatcacgcagtgctttctgcccgtgtttttggctcagcctccctcagggcaga ggcgctagtga 22IKASEKIFYVSLLMWITQCKASEKIFYVK Substrate in FIG. 9 23 VMTKLGFKVSSX-4₅₇₋₆₅ 24 RQIYVAAFTV PSMA₇₃₀₋₇₃₉ 25AQIPEKIQKAFDDIAKYFSKEEWEKMKASEKIFYVYMK SSX-2₁₅₋₁₈₃RKYEAMTKLGFKATLPPFMCNKRAEDFQGNDLDNDPNRGNQVERPQMTFGRLQGISPKIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWTH RLRERKQLVIYEEISDP 26MVMTKLGFKVKASEKIFYVRQIYVAAFTVGLPSIPVHP CTLS 1/pCBPITQCFLPVFLVMTKLGFKVRQIYVAAFTVKASEKIFYV expression productAQIPEKIQKAFDDIAKYFSKEEWEKMKASEKIFYVYMKRKYEAMTKLGFKATLPPFMCNKRAEDFQGNDLDNDPNRGNQVERPQMTFGRLQGISPKIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWTH RLRERKQLVIYEEISDP 27MAQIPEKIQKAFDDIAKYFSKEEWEKMKASEKIFYVYM CTLS2 expressionKRKYEAMTKLGFKATLPPFMCNKRAEDFQGNDLDNDPN productRGNQVERPQMTFGRLQGISPKIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWTHRLRERKQLVIYEEISDPVMTKLGFKVKASEKIFYVRQIYVAAFTVGLPSIPVHPITQCFLPVFLVMTKLGFKVRQ IYVAAFTVKASEKIFYV 28MVMTKLGFKVKASEKIFYVRQIYVAAFTVGLPSIPVHP CTLS3 expressionIAQIPEKIQKAFDDIAKYFSKEEWEKMKASEKIFYVYM productKRKYEAMTKLGFKATLPPFMCNKRAEDFQGNDLDNDPNRGNQVERPQMTFGRLQGISPKIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWT HRLRERKQLVIYEEISDP 29MAQIPEKIQKAFDDIAKYFSKEEWEKMKASEKIFYVYM CTLS4 expressionKRKYEAMTKLGFKATLPPFMCNKRAEDFQGNDLDNDPN productRGNQVERPQMTFGRLQGISPKIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWTHRLRERKQLVIYEEISDPTQCFLPVFLVMTKLGFKVRQ IYVAAFTVKASEKIFYV 30atggtcatgactaaactaggtttcaaggtcaaagcttc pCBP insert codingggagaaaatcttctatgtgagacagatttatgttgcag regionccttcacagtgggtcttccaagtattcctgttcatccaattacgcagtgctttctgcccgtgtttttggtcatgactaaactaggtttcaaggtcagacagatttatgttgcagccttcacagtgaaagcttcggagaaaatcttctacgtagctcaaataccagagaagatccaaaaggccttcgatgatattgccaaatacttctctaaggaagagtgggaaaagatgaaagcctcggagaaaatcttctatgtgtatatgaagagaaagtatgaggctatgactaaactaggtttcaaggccaccctcccacctttcatgtgtaataaacgggccgaagacttccaggggaatgatttggataatgaccctaaccgtgggaatcaggttgaacgtcctcagatgactttcggcaggctccagggaatctccccgaagatcatgcccaagaagccagcagaggaaggaaatgattcggaggaagtgccagaagcatctggcccacaaaatgatgggaaagagctgtgccccccgggaaaaccaactacctctgagaagattcacgagagatctggacccaaaaggggggaacatgcctggacccacagactgcgtgagagaaaacagctggtgatttatgaaga gatcagcgacccttagtga 31RQIYVAAFTVKASEKIFYVAQIPEKIQK FIG. 11 substrate/ CTLS1-2 32 FLPWHRLFLTYR₂₀₇₋₂₁₅ 33 MLLAVLYCLLWSFQTSAFLPWHRLFLMLLAVLYCLLWS CTLT2/pMELFQTSAFLPWHRLFLMLLAVLYCLLWSFQTSAFLPWHRL expression productFLMLLAVLYCLLWSFQTSAFLPWHRLFL 34 atgctcctggctgttttgtactgcctgctgtggagtttCTLT2/pMEL insert ccagacctccgcttttctgccttggcatagactcttct coding regiontgatgctcctggctgttttgtactgcctgctgtggagtttccagacctccgcttttctgccttggcatagactcttcttgatgctcctggctgttttgtactgcctgctgtggagtttccagacctccgcttttctgccttggcatagactcttcttgatgctcctggctgttttgtactgcctgctgtggagtttccagacctccgcttttctgccttggcatagac tcttcttgtagtga 35 MELAN-A cDNAAccession number: NM_005511 36 Tyrosinase cDNA Accession number:NM_000372 37 NY-ESO-1 cDNA Accession number: U87459 38 PSMA proteinAccession number: NP_004467 39 PSMA cDNA Accession number: NM_004476 40SSX-2 protein Accession number: NP_003138 41 SSX-2 cDNA Accessionnumber: NM_003147 42 atgacctctcgccgctccgtgaagtcgggtccgcggga Fromaccession number: ggttccgcgcgatgagtacgaggatctgtactacaccc D10879cgtcttcaggtatggcgagtcccgatagtccgcctgac Herpes Simplex virus 1acctcccgccgtggcgccctacagacacgctcgcgcca UL49 coding sequencegaggggcgaggtccgtttcgtccagtacgacgagtcgg (VP22)attatgccctctacgggggctcgtcatccgaagacgacgaacacccggaggtcccccggacgcggcgtcccgtttccggggcggttttgtccggcccggggcctgcgcgggcgcctccgccacccgctgggtccggaggggccggacgcacacccaccaccgccccccgggccccccgaacccagcgggtggcgactaaggcccccgcggccccggcggcggagaccacccgcggcaggaaatcggcccagccagaatccgccgcactcccagacgcccccgcgtcgacggcgccaacccgatccaagacacccgcgcaggggctggccagaaagctgcactttagcaccgcccccccaaaccccgacgcgccatggaccccccgggtggccggctttaacaagcgcgtcttctgcgccgcggtcgggcgcctggcggccatgcatgcccggatggcggcggtccagctctgggacatgtcgcgtccgcgcacagacgaagacctcaacgaactccttggcatcaccaccatccgcgtgacggtctgcgagggcaaaaacctgcttcagcgcgccaacgagttggtgaatccagacgtggtgcaggacgtcgacgcggccacggcgactcgagggcgttctgcggcgtcgcgccccaccgagcgacctcgagccccagcccgct ccgcttctcgccccagacggcccgtcgag 43MTSRRSVKSGPREVPRDEYEDLYYTPSSGMASPDSPPD Accession number:TSRRGALFTQTRSRQRGEVRFVQYDESDYALYGGSSSE P10233DDEHPEVPRTRRPVSGAVLSGPGPARAPPPFTPAGSGG Herpes Simplex virus 1AGRTPTTAPRAPRTQRVATKAPAAPAAETTRGRKSAQP UL49/VP22 proteinESAALPDAPASTAPTFTRSKTPAQGLARKLHFSTAPPN sequencePDAPWTPRVAGFNKRVFCAAVGRLAAMHARMAAVQLWDFTMSRPRTDEDLNELLGITTRIVTVCEGKNLLQRANELVNPDVVQDVDAATATRGRSAASRFTPTERPRAPARSAS RPRRPVE

[0205] Melan-A mRNA Sequence LOCUS NM_005511  1524 bp  mRNA  PRI  14OCT. 2001 DEFINITION Homo sapiens melan-A (MLANA), mRNA. ACCESSIONNM_005511 VERSION NM_005511.1 GI: 5031912 (SEQ ID NO. 2) /translation= “MPREDAHFIYGYPKKGHGHSYTTAEEAAGIGILTVILGVLLLIGCWYCRRRNGYRALMDKSLHVGTQCALTRRCPQEGFDHRDSKVSLQEKNCEPVVPNAPPAYEKLSAEQSPPPYSP” (SEQID NO. 35) ORIGIN    1 agcagacaga ggactctcat taaggaaggt gtcctgtgccctgaccctac aagatgccaa   61 gagaagatgc tcacttcatc tatggttacc ccaagaaggggcacggccac tcttacacca  121 cggctgaaga ggccgctggg atcggcatcc tgacagtgatcctgggagtc ttactgctca  181 tcggctgttg gtattgtaga agacgaaatg gatacagagccttgatggat aaaagtcttc  241 atgttggcac tcaatgtgcc ttaacaagaa gatgcccacaagaagggttt gatcatcggg  301 acagcaaagt gtctcttcaa gagaaaaact gtgaacctgtggttcccaat gctccacctg  361 cttatgagaa actctctgca gaacagtcac caccaccttattcaccttaa gagccagcga  421 gacacctgag acatgctgaa attatttctc tcacacttttgcttgaattt aatacagaca  481 tctaatgttc tcctttggaa tggtgtagga aaaatgcaagccatctctaa taataagtca  541 gtgttaaaat tttagtaggt ccgctagcag tactaatcatgtgaggaaat gatgagaaat  601 attaaattgg gaaaactcca tcaataaatg ttgcaatgcatgatactatc tgtgccagag  661 gtaatgttag taaatccatg gtgttatttt ctgagagacagaattcaagt gggtattctg  721 gggccatcca atttctcttt acttgaaatt tggctaataacaaactagtc aggttttcga  781 accttgaccg acatgaactg tacacagaat tgttccagtactatggagtg ctcacaaagg  841 atacttttac aggttaagac aaagggttga ctggcctatttatctgatca agaacatgtc  901 agcaatgtct ctttgtgctc taaaattcta ttatactacaataatatatt gtaaagatcc  961 tatagctctt tttttttgag atggagtttc gcttttgttgcccaggctgg agtgcaatgg 1021 cgcgatcttg gctcaccata acctccgcct cccaggttcaagcaattctc ctgccttagc 1081 ctcctgagta gctgggatta caggcgtgcg ccactatgcctgactaattt tgtagtttta 1141 gtagagacgg ggtttctcca tgttggtcag gctggtctcaaactcctgac ctcaggtgat 1201 ctgcccgcct cagcctccca aagtgctgga attacaggcgtgagccacca cgcctggctg 1261 gatcctatat cttaggtaag acatataacg cagtctaattacatttcact tcaaggctca 1321 atgctattct aactaatgac aagtattttc tactaaaccagaaattggta gaaggattta 1381 aataagtaaa agctactatg tactgcctta gtgctgatgcctgtgtactg ccttaaatgt 1441 acctatggca atttagctct cttgggttcc caaatccctctcacaagaat gtgcagaaga 1501 aatcataaag gatcagagat tctg

[0206] Tyrosinase mRNA Sequence LOCUS NM_000372  1964 bp  mRNA  PRI  31OCT. 2000 DEFINITION Homo sapiens tyrosinase (oculocutaneous albinismIA) (TYR), mRNA. ACCESSION NM_000372 VERSION NM_000372.1 GI: 4507752(SEQ ID NO. 3) /translation= “MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILLSNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVRRNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMHYYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRDAEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRNPGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLQEVYPEANAPIGHNRESYMVPFIPLYRNGDFFISSKDLGYDYSYLQDSDPDSFQDYIKSYLEQASRIWSWLLGAAMVGAVLTALLAGLVSLLCRHKRKQLP EEKQPLLMEKEDYHSLYQSHL” (SEQ IDNO. 36) ORIGIN    1 atcactgtag tagtagctgg aaagagaaat ctgtgactccaattagccag ttcctgcaga   61 ccttgtgagg actagaggaa gaatgctcct ggctgttttgtactgcctgc tgtggagttt  121 ccagacctcc gctggccatt tccctagagc ctgtgtctcctctaagaacc tgatggagaa  181 ggaatgctgt ccaccgtgga gcggggacag gagtccctgtggccagcttt caggcagagg  241 ttcctgtcag aatatccttc tgtccaatgc accacttgggcctcaatttc ccttcacagg  301 ggtggatgac cgggagtcgt ggccttccgt cttttataataggacctgcc agtgctctgg  361 caacttcatg ggattcaact gtggaaactg caagtttggcttttggggac caaactgcac  421 agagagacga ctcttggtga gaagaaacat cttcgatttgagtgccccag agaaggacaa  481 attttttgcc tacctcactt tagcaaagca taccatcagctcagactatg tcatccccat  541 agggacctat ggccaaatga aaaatggatc aacacccatgtttaacgaca tcaatattta  601 tgacctcttt gtctggatgc attattatgt gtcaatggatgcactgcttg ggggatctga  661 aatctggaga gacattgatt ttgcccatga agcaccagcttttctgcctt ggcatagact  721 cttcttgttg cggtgggaac aagaaatcca gaagctgacaggagatgaaa acttcactat  781 tccatattgg gactggcggg atgcagaaaa gtgtgacatttgcacagatg agtacatggg  841 aggtcagcac cccacaaatc ctaacttact cagcccagcatcattcttct cctcttggca  901 gattgtctgt agccgattgg aggagtacaa cagccatcagtctttatgca atggaacgcc  961 cgagggacct ttacggcgta atcctggaaa ccatgacaaatccagaaccc caaggctccc 1021 ctcttcagct gatgtagaat tttgcctgag tttgacccaatatgaatctg gttccatgga 1081 taaagctgcc aatttcagct ttagaaatac actggaaggatttgctagtc cacttactgg 1141 gatagcggat gcctctcaaa gcagcatgca caatgccttgcacatctata tgaatggaac 1201 aatgtcccag gtacagggat ctgccaacga tcctatcttccttcttcacc atgcatttgt 1261 tgacagtatt tttgagcagt ggctccgaag gcaccgtcctcttcaagaag tttatccaga 1321 agccaatgca cccattggac ataaccggga atcctacatggttcctttta taccactgta 1381 cagaaatggt gatttcttta tttcatccaa agatctgggctatgactata gctatctaca 1441 agattcagac ccagactctt ttcaagacta cattaagtcctatttggaac aagcgagtcg 1501 gatctggtca tggctccttg gggcggcgat ggtaggggccgtcctcactg ccctgctggc 1561 agggcttgtg agcttgctgt gtcgtcacaa gagaaagcagcttcctgaag aaaagcagcc 1621 actcctcatg gagaaagagg attaccacag cttgtatcagagccatttat aaaaggctta 1681 ggcaatagag tagggccaaa aagcctgacc tcactctaactcaaagtaat gtccaggttc 1741 ccagagaata tctgctggta tttttctgta aagaccatttgcaaaattgt aacctaatac 1801 aaagtgtagc cttcttccaa ctcaggtaga acacacctgtctttgtcttg ctgttttcac 1861 tcagcccttt taacattttc ccctaagccc atatgtctaaggaaaggatg ctatttggta 1921 atgaggaact gttatttgta tgtgaattaa agtgctcttatttt

[0207] (SEQ ID NO. 36) ORIGIN 1 atcactgtag tagtagctgg aaagagaaatctgtgactcc aattagccag ttcctgcaga 61 ccttgtgagg actagaggaa gaatgctcctggctgttttg tactgcctgc tgtggagttt 121 ccagacctcc gctggccatt tccctagagcctgtgtctcc tctaagaacc tgatggagaa 181 ggaatgctgt ccaccgtgga gcggggacaggagtccctgt ggccagcttt caggcagagg 241 ttcctgtcag aatatccttc tgtccaatgcaccacttggg cctcaatttc ccttcacagg 301 ggtggatgac cgggagtcgt ggccttccgtcttttataat aggacctgcc agtgctctgg 361 caacttcatg ggattcaact gtggaaactgcaagtttggc ttttggggac caaactgcac 421 agagagacga ctcttggtga gaagaaacatcttcgatttg agtgccccag agaaggacaa 481 attttttgcc tacctcactt tagcaaagcataccatcagc tcagactatg tcatccccat 541 agggacctat ggccaaatga aaaatggatcaacacccatg tttaacgaca tcaatattta 601 tgacctcttt gtctggatgc attattatgtgtcaatggat gcactgcttg ggggatctga 661 aatctggaga gacattgatt ttgcccatgaagcaccagct tttctgcctt ggcatagact 721 cttcttgttg cggtgggaac aagaaatccagaagctgaca ggagatgaaa acttcactat 781 tccatattgg gactggcggg atgcagaaaagtgtgacatt tgcacagatg agtacatggg 841 aggtcagcac cccacaaatc ctaacttactcagcccagca tcattcttct cctcttggca 901 gattgtctgt agccgattgg aggagtacaacagccatcag tctttatgca atggaacgcc 961 cgagggacct ttacggcgta atcctggaaaccatgacaaa tccagaaccc caaggctccc 1021 ctcttcagct gatgtagaat tttgcctgagtttgacccaa tatgaatctg gttccatgga 1081 taaagctgcc aatttcagct ttagaaatacactggaagga tttgctagtc cacttactgg 1141 gatagcggat gcctctcaaa gcagcatgcacaatgccttg cacatctata tgaatggaac 1201 aatgtcccag gtacagggat ctgccaacgatcctatcttc cttcttcacc atgcatttgt 1261 tgacagtatt tttgagcagt ggctccgaaggcaccgtcct cttcaagaag tttatccaga 1321 agccaatgca cccattggac ataaccgggaatcctacatg gttcctttta taccactgta 1381 cagaaatggt gatttcttta tttcatccaaagatctgggc tatgactata gctatctaca 1441 agattcagac ccagactctt ttcaagactacattaagtcc tatttggaac aagcgagtcg 1501 gatctggtca tggctccttg gggcggcgatggtaggggcc gtcctcactg ccctgctggc 1561 agggcttgtg agcttgctgt gtcgtcacaagagaaagcag cttcctgaag aaaagcagcc 1621 actcctcatg gagaaagagg attaccacagcttgtatcag agccatttat aaaaggctta 1681 ggcaatagag tagggccaaa aagcctgacctcactctaac tcaaagtaat gtccaggttc 1741 ccagagaata tctgctggta tttttctgtaaagaccattt gcaaaattgt aacctaatac 1801 aaagtgtagc cttcttccaa ctcaggtagaacacacctgt ctttgtcttg ctgttttcac 1861 tcagcccttt taacattttc ccctaagcccatatgtctaa ggaaaggatg ctatttggta 1921 atgaggaact gttatttgta tgtgaattaaagtgctctta tttt

[0208] NY-ESO-1 mRNA Sequence LOCUS HSU87459  752 bp  mRNA  PRI  22 DEC.1999 DEFINITION Human autoimmunogenic cancer/testis antigen NY-ESO-1mRNA, complete cds. ACCESSION U87459 VERSION U87459.1 GI: 1890098 (SEQID NO. 11) /translation= “MQAEGRGTGGSTGDADGPGGPGIPDGPGGNAGGPGEAGATGGRGPRGAGAARASGPGGGAPRGPHGGAASGLNGCCRCGARGPESRLLEFYLAMPFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNILTIRLTAADHRQLQLSISSCLQQLSLLMWITQCFLPVFLAQPPSGQRR” (SEQ ID NO.37) ORIGIN    1 atcctcgtgg gccctgacct tctctctgag agccgggcag aggctccggagccatgcagg   61 ccgaaggccg gggcacaggg ggttcgacgg gcgatgctga tggcccaggaggccctggca  121 ttcctgatgg cccagggggc aatgctggcg gcccaggaga ggcgggtgccacgggcggca  181 gaggtccccg gggcgcaggg gcagcaaggg cctcggggcc gggaggaggcgccccgcggg  241 gtccgcatgg cggcgcggct tcagggctga atggatgctg cagatgcggggccagggggc  301 cggagagccg cctgcttgag ttctacctcg ccatgccttt cgcgacacccatggaagcag  361 agctggcccg caggagcctg gcccaggatg ccccaccgct tcccgtgccaggggtgcttc  421 tgaaggagtt cactgtgtcc ggcaacatac tgactatccg actgactgctgcagaccacc  481 gccaactgca gctctccatc agctcctgtc tccagcagct ttccctgttgatgtggatca  541 cgcagtgctt tctgcccgtg tttttggctc agcctccctc agggcagaggcgctaagccc  601 agcctggcgc cccttcctag gtcatgcctc ctcccctagg gaatggtcccagcacgagtg  661 gccagttcat tgtgggggcc tgattgtttg tcgctggagg aggacggcttacatgtttgt  721 ttctgtagaa aataaaactg agctacgaaa aa

[0209] PSMA cDNA Sequence LOCUS NM_004476  2653 bp  mRNA  PRI  01 NOV.2000 DEFINITION Homo sapiens folate hydrolase (prostate-specificmembrane antigen) 1 (FOLH1), mRNA. ACCESSION NM_004476 VERSIONNM_004476.1 GI: 4758397 (SEQ ID NO. 38) /translation= “MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA”

[0210] (SEQ ID NO. 39) ORIGIN    1 ctcaaaaggg gccggatttc cttctcctggaggcagatgt tgcctctctc tctcgctcgg   61 attggttcag tgcactctag aaacactgctgtggtggaga aactggaccc caggtctgga  121 gcgaattcca gcctgcaggg ctgataagcgaggcattagt gagattgaga gagactttac  181 cccgccgtgg tggttggagg gcgcgcagtagagcagcagc acaggcgcgg gtcccgggag  241 gccggctctg ctcgcgccga gatgtggaatctccttcacg aaaccgactc ggctgtggcc  301 accgcgcgcc gcccgcgctg gctgtgcgctggggcgctgg tgctggcggg tggcttcttt  361 ctcctcggct tcctcttcgg gtggtttataaaatcctcca atgaagctac taacattact  421 ccaaagcata atatgaaagc atttttggatgaattgaaag ctgagaacat caagaagttc  481 ttatataatt ttacacagat accacatttagcaggaacag aacaaaactt tcagcttgca  541 aagcaaattc aatcccagtg gaaagaatttggcctggatt ctgttgagct agcacattat  601 gatgtcctgt tgtcctaccc aaataagactcatcccaact acatctcaat aattaatgaa  661 gatggaaatg agattttcaa cacatcattatttgaaccac ctcctccagg atatgaaaat  721 gtttcggata ttgtaccacc tttcagtgctttctctcctc aaggaatgcc agagggcgat  781 ctagtgtatg ttaactatgc acgaactgaagacttcttta aattggaacg ggacatgaaa  841 atcaattgct ctgggaaaat tgtaattgccagatatggga aagttttcag aggaaataag  901 gttaaaaatg cccagctggc aggggccaaaggagtcattc tctactccga ccctgctgac  961 tactttgctc ctggggtgaa gtcctatccagatggttgga atcttcctgg aggtggtgtc 1021 cagcgtggaa atatcctaaa tctgaatggtgcaggagacc ctctcacacc aggttaccca 1081 gcaaatgaat atgcttatag gcgtggaattgcagaggctg ttggtcttcc aagtattcct 1141 gttcatccaa ttggatacta tgatgcacagaagctcctag aaaaaatggg tggctcagca 1201 ccaccagata gcagctggag aggaagtctcaaagtgccct acaatgttgg acctggcttt 1261 actggaaact tttctacaca aaaagtcaagatgcacatcc actctaccaa tgaagtgaca 1321 agaatttaca atgtgatagg tactctcagaggagcagtgg aaccagacag atatgtcatt 1381 ctgggaggtc accgggactc atgggtgtttggtggtattg accctcagag tggagcagct 1441 gttgttcatg aaattgtgag gagctttggaacactgaaaa aggaagggtg gagacctaga 1501 agaacaattt tgtttgcaag ctgggatgcagaagaatttg gtcttcttgg ttctactgag 1561 tgggcagagg agaattcaag actccttcaagagcgtggcg tggcttatat taatgctgac 1621 tcatctatag aaggaaacta cactctgagagttgattgta caccgctgat gtacagcttg 1681 gtacacaacc taacaaaaga gctgaaaagccctgatgaag gctttgaagg caaatctctt 1741 tatgaaagtt ggactaaaaa aagtccttccccagagttca gtggcatgcc caggataagc 1801 aaattgggat ctggaaatga ttttgaggtgttcttccaac gacttggaat tgcttcaggc 1861 agagcacggt atactaaaaa ttgggaaacaaacaaattca gcggctatcc actgtatcac 1921 agtgtctatg aaacatatga gttggtggaaaagttttatg atccaatgtt taaatatcac 1981 ctcactgtgg cccaggttcg aggagggatggtgtttgagc tagccaattc catagtgctc 2041 ccttttgatt gtcgagatta tgctgtagttttaagaaagt atgctgacaa aatctacagt 2101 atttctatga aacatccaca ggaaatgaagacatacagtg tatcatttga ttcacttttt 2161 tctgcagtaa agaattttac agaaattgcttccaagttca gtgagagact ccaggacttt 2221 gacaaaagca acccaatagt attaagaatgatgaatgatc aactcatgtt tctggaaaga 2281 gcatttattg atccattagg gttaccagacaggccttttt ataggcatgt catctatgct 2341 ccaagcagcc acaacaagta tgcaggggagtcattcccag gaatttatga tgctctgttt 2401 gatattgaaa gcaaagtgga cccttccaaggcctggggag aagtgaagag acagatttat 2461 gttgcagcct tcacagtgca ggcagctgcagagactttga gtgaagtagc ctaagaggat 2521 tctttagaga atccgtattg aatttgtgtggtatgtcact cagaaagaat cgtaatgggt 2581 atattgataa attttaaaat tggtatatttgaaataaagt tgaatattat atataaaaaa 2641 aaaaaaaaaa aaa

[0211] NM_003147 Homo sapiens synovial sarcoma, X breakpoint 2 (SSX2),mRNA LOCUS NM_003147  766 bp  mRNA  PRI   14 MAR. 2001 DEFINITION Homosapiens synovial sarcoma, X breakpoint 2 (SSX2), mRNA. ACCESSIONNM_003147 VERSION NM_003147.1 GI: 10337582 SEQ ID NO. 40 /translation= “MNGDDAFARRPTVGAQIPEKIQKAFDDIAKYFSKEEWEKMKASEKIFYVYMKRKYEAMTKLGFKATLPPFMCNKRAEDFQGNDLDNDPNRGNQVERPQMTFGRLQGISPKIMPKKPAEEGNDSEEVPEASGPQNDGKELCPPGKPTTSEKIHERSGPKRGEHAWTHRLRERKQLVIYEEISDPEEDDE” SEQID NO. 41   1 ctctctttcg attcttccat actcagagta cgcacggtct gattttctctttggattctt  61 ccaaaatcag agtcagactg ctcccggtgc catgaacgga gacgacgcctttgcaaggag 121 acccacggtt ggtgctcaaa taccagagaa gatccaaaag gccttcgatgatattgccaa 181 atacttctct aaggaagagt gggaaaagat gaaagcctcg gagaaaatcttctatgtgta 241 tatgaagaga aagtatgagg ctatgactaa actaggtttc aaggccaccctcccaccttt 301 catgtgtaat aaacgggccg aagacttcca ggggaatgat ttggataatgaccctaaccg 361 tgggaatcag gttgaacgtc ctcagatgac tttcggcagg ctccagggaatctccccgaa 421 gatcatgccc aagaagccag cagaggaagg aaatgattcg gaggaagtgccagaagcatc 481 tggcccacaa aatgatggga aagagctgtg ccccccggga aaaccaactacctctgagaa 541 gattcacgag agatctggac ccaaaagggg ggaacatgcc tggacccacagactgcgtga 601 gagaaaacag ctggtgattt atgaagagat cagcgaccct gaggaagatgacgagtaact 661 cccctcaggg atacgacaca tgcccatgat gagaagcaga acgtggtgacctttcacgaa 721 catgggcatg gctgcggacc cctcgtcatc aggtgcatag caagtg

[0212]

1 979 1 10 PRT Homo Sapien 1 Glu Leu Ala Gly Ile Gly Ile Leu Thr Val 1 510 2 118 PRT Homo Sapien 2 Met Pro Arg Glu Asp Ala His Phe Ile Tyr GlyTyr Pro Lys Lys Gly 1 5 10 15 His Gly His Ser Tyr Thr Thr Ala Glu GluAla Ala Gly Ile Gly Ile 20 25 30 Leu Thr Val Ile Leu Gly Val Leu Leu LeuIle Gly Cys Trp Tyr Cys 35 40 45 Arg Arg Arg Asn Gly Tyr Arg Ala Leu MetAsp Lys Ser Leu His Val 50 55 60 Gly Thr Gln Cys Ala Leu Thr Arg Arg CysPro Gln Glu Gly Phe Asp 65 70 75 80 His Arg Asp Ser Lys Val Ser Leu GlnGlu Lys Asn Cys Glu Pro Val 85 90 95 Val Pro Asn Ala Pro Pro Ala Tyr GluLys Leu Ser Ala Glu Gln Ser 100 105 110 Pro Pro Pro Tyr Ser Pro 115 3529 PRT Homo Sapien 3 Met Leu Leu Ala Val Leu Tyr Cys Leu Leu Trp SerPhe Gln Thr Ser 1 5 10 15 Ala Gly His Phe Pro Arg Ala Cys Val Ser SerLys Asn Leu Met Glu 20 25 30 Lys Glu Cys Cys Pro Pro Trp Ser Gly Asp ArgSer Pro Cys Gly Gln 35 40 45 Leu Ser Gly Arg Gly Ser Cys Gln Asn Ile LeuLeu Ser Asn Ala Pro 50 55 60 Leu Gly Pro Gln Phe Pro Phe Thr Gly Val AspAsp Arg Glu Ser Trp 65 70 75 80 Pro Ser Val Phe Tyr Asn Arg Thr Cys GlnCys Ser Gly Asn Phe Met 85 90 95 Gly Phe Asn Cys Gly Asn Cys Lys Phe GlyPhe Trp Gly Pro Asn Cys 100 105 110 Thr Glu Arg Arg Leu Leu Val Arg ArgAsn Ile Phe Asp Leu Ser Ala 115 120 125 Pro Glu Lys Asp Lys Phe Phe AlaTyr Leu Thr Leu Ala Lys His Thr 130 135 140 Ile Ser Ser Asp Tyr Val IlePro Ile Gly Thr Tyr Gly Gln Met Lys 145 150 155 160 Asn Gly Ser Thr ProMet Phe Asn Asp Ile Asn Ile Tyr Asp Leu Phe 165 170 175 Val Trp Met HisTyr Tyr Val Ser Met Asp Ala Leu Leu Gly Gly Ser 180 185 190 Glu Ile TrpArg Asp Ile Asp Phe Ala His Glu Ala Pro Ala Phe Leu 195 200 205 Pro TrpHis Arg Leu Phe Leu Leu Arg Trp Glu Gln Glu Ile Gln Lys 210 215 220 LeuThr Gly Asp Glu Asn Phe Thr Ile Pro Tyr Trp Asp Trp Arg Asp 225 230 235240 Ala Glu Lys Cys Asp Ile Cys Thr Asp Glu Tyr Met Gly Gly Gln His 245250 255 Pro Thr Asn Pro Asn Leu Leu Ser Pro Ala Ser Phe Phe Ser Ser Trp260 265 270 Gln Ile Val Cys Ser Arg Leu Glu Glu Tyr Asn Ser His Gln SerLeu 275 280 285 Cys Asn Gly Thr Pro Glu Gly Pro Leu Arg Arg Asn Pro GlyAsn His 290 295 300 Asp Lys Ser Arg Thr Pro Arg Leu Pro Ser Ser Ala AspVal Glu Phe 305 310 315 320 Cys Leu Ser Leu Thr Gln Tyr Glu Ser Gly SerMet Asp Lys Ala Ala 325 330 335 Asn Phe Ser Phe Arg Asn Thr Leu Glu GlyPhe Ala Ser Pro Leu Thr 340 345 350 Gly Ile Ala Asp Ala Ser Gln Ser SerMet His Asn Ala Leu His Ile 355 360 365 Tyr Met Asn Gly Thr Met Ser GlnVal Gln Gly Ser Ala Asn Asp Pro 370 375 380 Ile Phe Leu Leu His His AlaPhe Val Asp Ser Ile Phe Glu Gln Trp 385 390 395 400 Leu Arg Arg His ArgPro Leu Gln Glu Val Tyr Pro Glu Ala Asn Ala 405 410 415 Pro Ile Gly HisAsn Arg Glu Ser Tyr Met Val Pro Phe Ile Pro Leu 420 425 430 Tyr Arg AsnGly Asp Phe Phe Ile Ser Ser Lys Asp Leu Gly Tyr Asp 435 440 445 Tyr SerTyr Leu Gln Asp Ser Asp Pro Asp Ser Phe Gln Asp Tyr Ile 450 455 460 LysSer Tyr Leu Glu Gln Ala Ser Arg Ile Trp Ser Trp Leu Leu Gly 465 470 475480 Ala Ala Met Val Gly Ala Val Leu Thr Ala Leu Leu Ala Gly Leu Val 485490 495 Ser Leu Leu Cys Arg His Lys Arg Lys Gln Leu Pro Glu Glu Lys Gln500 505 510 Pro Leu Leu Met Glu Lys Glu Asp Tyr His Ser Leu Tyr Gln SerHis 515 520 525 Leu 4 94 PRT Artificial Sequence pMA2M expressionproduct 4 Met Leu Leu Ala Val Leu Tyr Cys Leu Glu Leu Ala Gly Ile GlyIle 1 5 10 15 Leu Thr Val Tyr Met Asp Gly Thr Met Ser Gln Val Gly IleLeu Thr 20 25 30 Val Ile Leu Gly Val Leu Leu Leu Ile Gly Cys Trp Tyr CysArg Arg 35 40 45 Arg Asn Gly Tyr Arg Ala Leu Met Asp Lys Ser Leu His ValGly Thr 50 55 60 Gln Cys Ala Leu Thr Arg Arg Cys Pro Gln Glu Gly Phe AspHis Arg 65 70 75 80 Asp Ser Lys Val Ser Leu Gln Glu Lys Asn Cys Glu ProVal 85 90 5 28 PRT Artificial Sequence Epitope liberation sequence forSEQ ID NO. 1 from pMA2M 5 Met Leu Leu Ala Val Leu Tyr Cys Leu Glu LeuAla Gly Ile Gly Ile 1 5 10 15 Leu Thr Val Tyr Met Asp Gly Thr Met SerGln Val 20 25 6 9 PRT Homo Sapien 6 Met Leu Leu Ala Val Leu Tyr Cys Leu1 5 7 9 PRT Homo Sapien 7 Tyr Met Asp Gly Thr Met Ser Gln Val 1 5 8 10PRT Homo Sapien 8 Glu Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5 10 9 307DNA Artificial Sequence pMA2M insert coding region 9 cttaagccaccatgttacta gctgttttgt actgcctgga actagcaggg atcggcatat 60 tgacagtgtatatggatgga acaatgtccc aggtaggaat tctgacagtg atcctgggag 120 tcttactgctcatcggctgt tggtattgta gaagacgaaa tggatacaga gccttgatgg 180 ataaaagtcttcatgttggc actcaatgtg ccttaacaag aagatgccca caagaagggt 240 ttgatcatcgggacagcaaa gtgtctcttc aagagaaaaa ctgtgaacct gtgtagtgag 300 cggccgc 30710 85 PRT Artificial Sequence Epitope array from pVAXM2 and pVAXM1 10Met Val Leu Tyr Cys Leu Glu Leu Ala Gly Ile Gly Ile Leu Thr Val 1 5 1015 Tyr Met Asp Gly Thr Ala Val Leu Tyr Cys Leu Glu Leu Ala Gly Ile 20 2530 Gly Ile Leu Thr Val Tyr Met Asp Gly Thr Met Leu Ala Val Leu Tyr 35 4045 Cys Leu Glu Leu Ala Gly Ile Gly Ile Leu Thr Val Tyr Met Asp Gly 50 5560 Thr Met Ser Leu Leu Ala Val Leu Tyr Cys Leu Glu Leu Ala Gly Ile 65 7075 80 Gly Ile Leu Thr Val 85 11 180 PRT Homo Sapien 11 Met Gln Ala GluGly Arg Gly Thr Gly Gly Ser Thr Gly Asp Ala Asp 1 5 10 15 Gly Pro GlyGly Pro Gly Ile Pro Asp Gly Pro Gly Gly Asn Ala Gly 20 25 30 Gly Pro GlyGlu Ala Gly Ala Thr Gly Gly Arg Gly Pro Arg Gly Ala 35 40 45 Gly Ala AlaArg Ala Ser Gly Pro Gly Gly Gly Ala Pro Arg Gly Pro 50 55 60 His Gly GlyAla Ala Ser Gly Leu Asn Gly Cys Cys Arg Cys Gly Ala 65 70 75 80 Arg GlyPro Glu Ser Arg Leu Leu Glu Phe Tyr Leu Ala Met Pro Phe 85 90 95 Ala ThrPro Met Glu Ala Glu Leu Ala Arg Arg Ser Leu Ala Gln Asp 100 105 110 AlaPro Pro Leu Pro Val Pro Gly Val Leu Leu Lys Glu Phe Thr Val 115 120 125Ser Gly Asn Ile Leu Thr Ile Arg Leu Thr Ala Ala Asp His Arg Gln 130 135140 Leu Gln Leu Ser Ile Ser Ser Cys Leu Gln Gln Leu Ser Leu Leu Met 145150 155 160 Trp Ile Thr Gln Cys Phe Leu Pro Val Phe Leu Ala Gln Pro ProSer 165 170 175 Gly Gln Arg Arg 180 12 9 PRT Homo Sapien 12 Ser Leu LeuMet Trp Ile Thr Gln Cys 1 5 13 9 PRT Homo Sapien 13 Lys Ala Ser Glu LysIle Phe Tyr Val 1 5 14 9 PRT Homo Sapien 14 Thr Gln Cys Phe Leu Pro ValPhe Leu 1 5 15 10 PRT Homo Sapien 15 Gly Leu Pro Ser Ile Pro Val His ProIle 1 5 10 16 6 PRT Homo Sapien 16 Ala Val Leu Tyr Cys Leu 1 5 17 123PRT Artificial Sequence pN157 expression product 17 Met Ser Leu Leu MetTrp Ile Thr Gln Cys Lys Ala Ser Glu Lys Ile 1 5 10 15 Phe Tyr Val ArgCys Gly Ala Arg Gly Pro Glu Ser Arg Leu Leu Glu 20 25 30 Phe Tyr Leu AlaMet Pro Phe Ala Thr Pro Met Glu Ala Glu Leu Ala 35 40 45 Arg Arg Ser LeuAla Gln Asp Ala Pro Pro Leu Pro Val Pro Gly Val 50 55 60 Leu Leu Lys GluPhe Thr Val Ser Gly Asn Ile Leu Thr Ile Arg Leu 65 70 75 80 Thr Ala AlaAsp His Arg Gln Leu Gln Leu Ser Ile Ser Ser Cys Leu 85 90 95 Gln Gln LeuSer Leu Leu Met Trp Ile Thr Gln Cys Phe Leu Pro Val 100 105 110 Phe LeuAla Gln Pro Pro Ser Gly Gln Arg Arg 115 120 18 19 PRT ArtificialSequence Epitope liberation sequence for SEQ ID NO. 12 from pN157 18 MetSer Leu Leu Met Trp Ile Thr Gln Cys Lys Ala Ser Glu Lys Ile 1 5 10 15Phe Tyr Val 19 392 DNA Artificial Sequence pN157 insert coding region 19cttaagccac catgtccctg ttgatgtgga tcacgcagtg caaagcttcg gagaaaatct 60tctacgtacg gtgcggtgcc agggggccgg agagccgcct gcttgagttc tacctcgcca 120tgcctttcgc gacacccatg gaagcagagc tggcccgcag gagcctggcc caggatgccc 180caccgcttcc cgtgccaggg gtgcttctga aggagttcac tgtgtccggc aacatactga 240ctatccgact gactgctgca gaccaccgcc aactgcagct ctccatcagc tcctgtctcc 300agcagctttc cctgttgatg tggatcacgc agtgctttct gcccgtgttt ttggctcagc 360ctccctcagg gcagaggcgc tagtgagaat tc 392 20 179 PRT Artificial SequencepBPL expression product 20 Met Ser Leu Leu Met Trp Ile Thr Gln Cys LysAla Ser Glu Lys Ile 1 5 10 15 Phe Tyr Val Gly Leu Pro Ser Ile Pro ValHis Pro Ile Gly Leu Pro 20 25 30 Ser Ile Pro Val His Pro Ile Lys Ala SerGlu Lys Ile Phe Tyr Val 35 40 45 Ser Leu Leu Met Trp Ile Thr Gln Cys LysAla Ser Glu Lys Ile Phe 50 55 60 Tyr Val Lys Ala Ser Glu Lys Ile Phe TyrVal Arg Cys Gly Ala Arg 65 70 75 80 Gly Pro Glu Ser Arg Leu Leu Glu PheTyr Leu Ala Met Pro Phe Ala 85 90 95 Thr Pro Met Glu Ala Glu Leu Ala ArgArg Ser Leu Ala Gln Asp Ala 100 105 110 Pro Pro Leu Pro Val Pro Gly ValLeu Leu Lys Glu Phe Thr Val Ser 115 120 125 Gly Asn Ile Leu Thr Ile ArgLeu Thr Ala Ala Asp His Arg Gln Leu 130 135 140 Gln Leu Ser Ile Ser SerCys Leu Gln Gln Leu Ser Leu Leu Met Trp 145 150 155 160 Ile Thr Gln CysPhe Leu Pro Val Phe Leu Ala Gln Pro Pro Ser Gly 165 170 175 Gln Arg Arg21 543 DNA Artificial Sequence pBPL insert coding region 21 atgtccctgttgatgtggat cacgcagtgc aaagcttcgg agaaaatctt ctatgtgggt 60 cttccaagtattcctgttca tccaattggt cttccaagta ttcctgttca tccaattaaa 120 gcttcggagaaaatcttcta tgtgtccctg ttgatgtgga tcacgcagtg caaagcttcg 180 gagaaaatcttctatgtgaa agcttcggag aaaatcttct acgtacggtg cggtgccagg 240 gggccggagagccgcctgct tgagttctac ctcgccatgc ctttcgcgac acccatggaa 300 gcagagctggcccgcaggag cctggcccag gatgccccac cgcttcccgt gccaggggtg 360 cttctgaaggagttcactgt gtccggcaac atactgacta tccgactgac tgctgcagac 420 caccgccaactgcagctctc catcagctcc tgtctccagc agctttccct gttgatgtgg 480 atcacgcagtgctttctgcc cgtgtttttg gctcagcctc cctcagggca gaggcgctag 540 tga 543 22 29PRT Artificial Sequence liberation sequence for SEQ ID NO. 22 22 Ile LysAla Ser Glu Lys Ile Phe Tyr Val Ser Leu Leu Met Trp Ile 1 5 10 15 ThrGln Cys Lys Ala Ser Glu Lys Ile Phe Tyr Val Lys 20 25 23 9 PRT HomoSapien 23 Val Met Thr Lys Leu Gly Phe Lys Val 1 5 24 10 PRT Homo Sapien24 Arg Gln Ile Tyr Val Ala Ala Phe Thr Val 1 5 10 25 169 PRT Homo Sapien25 Ala Gln Ile Pro Glu Lys Ile Gln Lys Ala Phe Asp Asp Ile Ala Lys 1 510 15 Tyr Phe Ser Lys Glu Glu Trp Glu Lys Met Lys Ala Ser Glu Lys Ile 2025 30 Phe Tyr Val Tyr Met Lys Arg Lys Tyr Glu Ala Met Thr Lys Leu Gly 3540 45 Phe Lys Ala Thr Leu Pro Pro Phe Met Cys Asn Lys Arg Ala Glu Asp 5055 60 Phe Gln Gly Asn Asp Leu Asp Asn Asp Pro Asn Arg Gly Asn Gln Val 6570 75 80 Glu Arg Pro Gln Met Thr Phe Gly Arg Leu Gln Gly Ile Ser Pro Lys85 90 95 Ile Met Pro Lys Lys Pro Ala Glu Glu Gly Asn Asp Ser Glu Glu Val100 105 110 Pro Glu Ala Ser Gly Pro Gln Asn Asp Gly Lys Glu Leu Cys ProPro 115 120 125 Gly Lys Pro Thr Thr Ser Glu Lys Ile His Glu Arg Ser GlyPro Lys 130 135 140 Arg Gly Glu His Ala Trp Thr His Arg Leu Arg Glu ArgLys Gln Leu 145 150 155 160 Val Ile Tyr Glu Glu Ile Ser Asp Pro 165 26245 PRT Artificial Sequence CTLS1/pCBP expression product 26 Met Val MetThr Lys Leu Gly Phe Lys Val Lys Ala Ser Glu Lys Ile 1 5 10 15 Phe TyrVal Arg Gln Ile Tyr Val Ala Ala Phe Thr Val Gly Leu Pro 20 25 30 Ser IlePro Val His Pro Ile Thr Gln Cys Phe Leu Pro Val Phe Leu 35 40 45 Val MetThr Lys Leu Gly Phe Lys Val Arg Gln Ile Tyr Val Ala Ala 50 55 60 Phe ThrVal Lys Ala Ser Glu Lys Ile Phe Tyr Val Ala Gln Ile Pro 65 70 75 80 GluLys Ile Gln Lys Ala Phe Asp Asp Ile Ala Lys Tyr Phe Ser Lys 85 90 95 GluGlu Trp Glu Lys Met Lys Ala Ser Glu Lys Ile Phe Tyr Val Tyr 100 105 110Met Lys Arg Lys Tyr Glu Ala Met Thr Lys Leu Gly Phe Lys Ala Thr 115 120125 Leu Pro Pro Phe Met Cys Asn Lys Arg Ala Glu Asp Phe Gln Gly Asn 130135 140 Asp Leu Asp Asn Asp Pro Asn Arg Gly Asn Gln Val Glu Arg Pro Gln145 150 155 160 Met Thr Phe Gly Arg Leu Gln Gly Ile Ser Pro Lys Ile MetPro Lys 165 170 175 Lys Pro Ala Glu Glu Gly Asn Asp Ser Glu Glu Val ProGlu Ala Ser 180 185 190 Gly Pro Gln Asn Asp Gly Lys Glu Leu Cys Pro ProGly Lys Pro Thr 195 200 205 Thr Ser Glu Lys Ile His Glu Arg Ser Gly ProLys Arg Gly Glu His 210 215 220 Ala Trp Thr His Arg Leu Arg Glu Arg LysGln Leu Val Ile Tyr Glu 225 230 235 240 Glu Ile Ser Asp Pro 245 27 245PRT Artificial Sequence CTL52 expression product 27 Met Ala Gln Ile ProGlu Lys Ile Gln Lys Ala Phe Asp Asp Ile Ala 1 5 10 15 Lys Tyr Phe SerLys Glu Glu Trp Glu Lys Met Lys Ala Ser Glu Lys 20 25 30 Ile Phe Tyr ValTyr Met Lys Arg Lys Tyr Glu Ala Met Thr Lys Leu 35 40 45 Gly Phe Lys AlaThr Leu Pro Pro Phe Met Cys Asn Lys Arg Ala Glu 50 55 60 Asp Phe Gln GlyAsn Asp Leu Asp Asn Asp Pro Asn Arg Gly Asn Gln 65 70 75 80 Val Glu ArgPro Gln Met Thr Phe Gly Arg Leu Gln Gly Ile Ser Pro 85 90 95 Lys Ile MetPro Lys Lys Pro Ala Glu Glu Gly Asn Asp Ser Glu Glu 100 105 110 Val ProGlu Ala Ser Gly Pro Gln Asn Asp Gly Lys Glu Leu Cys Pro 115 120 125 ProGly Lys Pro Thr Thr Ser Glu Lys Ile His Glu Arg Ser Gly Pro 130 135 140Lys Arg Gly Glu His Ala Trp Thr His Arg Leu Arg Glu Arg Lys Gln 145 150155 160 Leu Val Ile Tyr Glu Glu Ile Ser Asp Pro Val Met Thr Lys Leu Gly165 170 175 Phe Lys Val Lys Ala Ser Glu Lys Ile Phe Tyr Val Arg Gln IleTyr 180 185 190 Val Ala Ala Phe Thr Val Gly Leu Pro Ser Ile Pro Val HisPro Ile 195 200 205 Thr Gln Cys Phe Leu Pro Val Phe Leu Val Met Thr LysLeu Gly Phe 210 215 220 Lys Val Arg Gln Ile Tyr Val Ala Ala Phe Thr ValLys Ala Ser Glu 225 230 235 240 Lys Ile Phe Tyr Val 245 28 208 PRTArtificial Sequence CTL53 expression product 28 Met Val Met Thr Lys LeuGly Phe Lys Val Lys Ala Ser Glu Lys Ile 1 5 10 15 Phe Tyr Val Arg GlnIle Tyr Val Ala Ala Phe Thr Val Gly Leu Pro 20 25 30 Ser Ile Pro Val HisPro Ile Ala Gln Ile Pro Glu Lys Ile Gln Lys 35 40 45 Ala Phe Asp Asp IleAla Lys Tyr Phe Ser Lys Glu Glu Trp Glu Lys 50 55 60 Met Lys Ala Ser GluLys Ile Phe Tyr Val Tyr Met Lys Arg Lys Tyr 65 70 75 80 Glu Ala Met ThrLys Leu Gly Phe Lys Ala Thr Leu Pro Pro Phe Met 85 90 95 Cys Asn Lys ArgAla Glu Asp Phe Gln Gly Asn Asp Leu Asp Asn Asp 100 105 110 Pro Asn ArgGly Asn Gln Val Glu Arg Pro Gln Met Thr Phe Gly Arg 115 120 125 Leu GlnGly Ile Ser Pro Lys Ile Met Pro Lys Lys Pro Ala Glu Glu 130 135 140 GlyAsn Asp Ser Glu Glu Val Pro Glu Ala Ser Gly Pro Gln Asn Asp 145 150 155160 Gly Lys Glu Leu Cys Pro Pro Gly Lys Pro Thr Thr Ser Glu Lys Ile 165170 175 His Glu Arg Ser Gly Pro Lys Arg Gly Glu His Ala Trp Thr His Arg180 185 190 Leu Arg Glu Arg Lys Gln Leu Val Ile Tyr Glu Glu Ile Ser AspPro 195 200 205 29 207 PRT Artificial Sequence CTL54 expression product29 Met Ala Gln Ile Pro Glu Lys Ile Gln Lys Ala Phe Asp Asp Ile Ala 1 510 15 Lys Tyr Phe Ser Lys Glu Glu Trp Glu Lys Met Lys Ala Ser Glu Lys 2025 30 Ile Phe Tyr Val Tyr Met Lys Arg Lys Tyr Glu Ala Met Thr Lys Leu 3540 45 Gly Phe Lys Ala Thr Leu Pro Pro Phe Met Cys Asn Lys Arg Ala Glu 5055 60 Asp Phe Gln Gly Asn Asp Leu Asp Asn Asp Pro Asn Arg Gly Asn Gln 6570 75 80 Val Glu Arg Pro Gln Met Thr Phe Gly Arg Leu Gln Gly Ile Ser Pro85 90 95 Lys Ile Met Pro Lys Lys Pro Ala Glu Glu Gly Asn Asp Ser Glu Glu100 105 110 Val Pro Glu Ala Ser Gly Pro Gln Asn Asp Gly Lys Glu Leu CysPro 115 120 125 Pro Gly Lys Pro Thr Thr Ser Glu Lys Ile His Glu Arg SerGly Pro 130 135 140 Lys Arg Gly Glu His Ala Trp Thr His Arg Leu Arg GluArg Lys Gln 145 150 155 160 Leu Val Ile Tyr Glu Glu Ile Ser Asp Pro ThrGln Cys Phe Leu Pro 165 170 175 Val Phe Leu Val Met Thr Lys Leu Gly PheLys Val Arg Gln Ile Tyr 180 185 190 Val Ala Ala Phe Thr Val Lys Ala SerGlu Lys Ile Phe Tyr Val 195 200 205 30 741 DNA Artificial Sequence pCBPinsert coding region 30 atggtcatga ctaaactagg tttcaaggtc aaagcttcggagaaaatctt ctatgtgaga 60 cagatttatg ttgcagcctt cacagtgggt cttccaagtattcctgttca tccaattacg 120 cagtgctttc tgcccgtgtt tttggtcatg actaaactaggtttcaaggt cagacagatt 180 tatgttgcag ccttcacagt gaaagcttcg gagaaaatcttctacgtagc tcaaatacca 240 gagaagatcc aaaaggcctt cgatgatatt gccaaatacttctctaagga agagtgggaa 300 aagatgaaag cctcggagaa aatcttctat gtgtatatgaagagaaagta tgaggctatg 360 actaaactag gtttcaaggc caccctccca cctttcatgtgtaataaacg ggccgaagac 420 ttccagggga atgatttgga taatgaccct aaccgtgggaatcaggttga acgtcctcag 480 atgactttcg gcaggctcca gggaatctcc ccgaagatcatgcccaagaa gccagcagag 540 gaaggaaatg attcggagga agtgccagaa gcatctggcccacaaaatga tgggaaagag 600 ctgtgccccc cgggaaaacc aactacctct gagaagattcacgagagatc tggacccaaa 660 aggggggaac atgcctggac ccacagactg cgtgagagaaaacagctggt gatttatgaa 720 gagatcagcg acccttagtg a 741 31 28 PRTArtificial Sequence CTLS11-2 liberation/substrate sequence 31 Arg GlnIle Tyr Val Ala Ala Phe Thr Val Lys Ala Ser Glu Lys Ile 1 5 10 15 PheTyr Val Ala Gln Ile Pro Glu Lys Ile Gln Lys 20 25 32 9 PRT Homo Sapien32 Phe Leu Pro Trp His Arg Leu Phe Leu 1 5 33 104 PRT ArtificialSequence CTLT2/pMEL expression product 33 Met Leu Leu Ala Val Leu TyrCys Leu Leu Trp Ser Phe Gln Thr Ser 1 5 10 15 Ala Phe Leu Pro Trp HisArg Leu Phe Leu Met Leu Leu Ala Val Leu 20 25 30 Tyr Cys Leu Leu Trp SerPhe Gln Thr Ser Ala Phe Leu Pro Trp His 35 40 45 Arg Leu Phe Leu Met LeuLeu Ala Val Leu Tyr Cys Leu Leu Trp Ser 50 55 60 Phe Gln Thr Ser Ala PheLeu Pro Trp His Arg Leu Phe Leu Met Leu 65 70 75 80 Leu Ala Val Leu TyrCys Leu Leu Trp Ser Phe Gln Thr Ser Ala Phe 85 90 95 Leu Pro Trp His ArgLeu Phe Leu 100 34 318 DNA Artificial Sequence CTLT2/pMEL insert codingregion 34 atgctcctgg ctgttttgta ctgcctgctg tggagtttcc agacctccgcttttctgcct 60 tggcatagac tcttcttgat gctcctggct gttttgtact gcctgctgtggagtttccag 120 acctccgctt ttctgccttg gcatagactc ttcttgatgc tcctggctgttttgtactgc 180 ctgctgtgga gtttccagac ctccgctttt ctgccttggc atagactcttcttgatgctc 240 ctggctgttt tgtactgcct gctgtggagt ttccagacct ccgcttttctgccttggcat 300 agactcttct tgtagtga 318 35 1524 DNA Homo Sapien 35agcagacaga ggactctcat taaggaaggt gtcctgtgcc ctgaccctac aagatgccaa 60gagaagatgc tcacttcatc tatggttacc ccaagaaggg gcacggccac tcttacacca 120cggctgaaga ggccgctggg atcggcatcc tgacagtgat cctgggagtc ttactgctca 180tcggctgttg gtattgtaga agacgaaatg gatacagagc cttgatggat aaaagtcttc 240atgttggcac tcaatgtgcc ttaacaagaa gatgcccaca agaagggttt gatcatcggg 300acagcaaagt gtctcttcaa gagaaaaact gtgaacctgt ggttcccaat gctccacctg 360cttatgagaa actctctgca gaacagtcac caccacctta ttcaccttaa gagccagcga 420gacacctgag acatgctgaa attatttctc tcacactttt gcttgaattt aatacagaca 480tctaatgttc tcctttggaa tggtgtagga aaaatgcaag ccatctctaa taataagtca 540gtgttaaaat tttagtaggt ccgctagcag tactaatcat gtgaggaaat gatgagaaat 600attaaattgg gaaaactcca tcaataaatg ttgcaatgca tgatactatc tgtgccagag 660gtaatgttag taaatccatg gtgttatttt ctgagagaca gaattcaagt gggtattctg 720gggccatcca atttctcttt acttgaaatt tggctaataa caaactagtc aggttttcga 780accttgaccg acatgaactg tacacagaat tgttccagta ctatggagtg ctcacaaagg 840atacttttac aggttaagac aaagggttga ctggcctatt tatctgatca agaacatgtc 900agcaatgtct ctttgtgctc taaaattcta ttatactaca ataatatatt gtaaagatcc 960tatagctctt tttttttgag atggagtttc gcttttgttg cccaggctgg agtgcaatgg 1020cgcgatcttg gctcaccata acctccgcct cccaggttca agcaattctc ctgccttagc 1080ctcctgagta gctgggatta caggcgtgcg ccactatgcc tgactaattt tgtagtttta 1140gtagagacgg ggtttctcca tgttggtcag gctggtctca aactcctgac ctcaggtgat 1200ctgcccgcct cagcctccca aagtgctgga attacaggcg tgagccacca cgcctggctg 1260gatcctatat cttaggtaag acatataacg cagtctaatt acatttcact tcaaggctca 1320atgctattct aactaatgac aagtattttc tactaaacca gaaattggta gaaggattta 1380aataagtaaa agctactatg tactgcctta gtgctgatgc ctgtgtactg ccttaaatgt 1440acctatggca atttagctct cttgggttcc caaatccctc tcacaagaat gtgcagaaga 1500aatcataaag gatcagagat tctg 1524 36 1964 DNA Homo Sapien 36 atcactgtagtagtagctgg aaagagaaat ctgtgactcc aattagccag ttcctgcaga 60 ccttgtgaggactagaggaa gaatgctcct ggctgttttg tactgcctgc tgtggagttt 120 ccagacctccgctggccatt tccctagagc ctgtgtctcc tctaagaacc tgatggagaa 180 ggaatgctgtccaccgtgga gcggggacag gagtccctgt ggccagcttt caggcagagg 240 ttcctgtcagaatatccttc tgtccaatgc accacttggg cctcaatttc ccttcacagg 300 ggtggatgaccgggagtcgt ggccttccgt cttttataat aggacctgcc agtgctctgg 360 caacttcatgggattcaact gtggaaactg caagtttggc ttttggggac caaactgcac 420 agagagacgactcttggtga gaagaaacat cttcgatttg agtgccccag agaaggacaa 480 attttttgcctacctcactt tagcaaagca taccatcagc tcagactatg tcatccccat 540 agggacctatggccaaatga aaaatggatc aacacccatg tttaacgaca tcaatattta 600 tgacctctttgtctggatgc attattatgt gtcaatggat gcactgcttg ggggatctga 660 aatctggagagacattgatt ttgcccatga agcaccagct tttctgcctt ggcatagact 720 cttcttgttgcggtgggaac aagaaatcca gaagctgaca ggagatgaaa acttcactat 780 tccatattgggactggcggg atgcagaaaa gtgtgacatt tgcacagatg agtacatggg 840 aggtcagcaccccacaaatc ctaacttact cagcccagca tcattcttct cctcttggca 900 gattgtctgtagccgattgg aggagtacaa cagccatcag tctttatgca atggaacgcc 960 cgagggacctttacggcgta atcctggaaa ccatgacaaa tccagaaccc caaggctccc 1020 ctcttcagctgatgtagaat tttgcctgag tttgacccaa tatgaatctg gttccatgga 1080 taaagctgccaatttcagct ttagaaatac actggaagga tttgctagtc cacttactgg 1140 gatagcggatgcctctcaaa gcagcatgca caatgccttg cacatctata tgaatggaac 1200 aatgtcccaggtacagggat ctgccaacga tcctatcttc cttcttcacc atgcatttgt 1260 tgacagtatttttgagcagt ggctccgaag gcaccgtcct cttcaagaag tttatccaga 1320 agccaatgcacccattggac ataaccggga atcctacatg gttcctttta taccactgta 1380 cagaaatggtgatttcttta tttcatccaa agatctgggc tatgactata gctatctaca 1440 agattcagacccagactctt ttcaagacta cattaagtcc tatttggaac aagcgagtcg 1500 gatctggtcatggctccttg gggcggcgat ggtaggggcc gtcctcactg ccctgctggc 1560 agggcttgtgagcttgctgt gtcgtcacaa gagaaagcag cttcctgaag aaaagcagcc 1620 actcctcatggagaaagagg attaccacag cttgtatcag agccatttat aaaaggctta 1680 ggcaatagagtagggccaaa aagcctgacc tcactctaac tcaaagtaat gtccaggttc 1740 ccagagaatatctgctggta tttttctgta aagaccattt gcaaaattgt aacctaatac 1800 aaagtgtagccttcttccaa ctcaggtaga acacacctgt ctttgtcttg ctgttttcac 1860 tcagcccttttaacattttc ccctaagccc atatgtctaa ggaaaggatg ctatttggta 1920 atgaggaactgttatttgta tgtgaattaa agtgctctta tttt 1964 37 752 DNA Homo Sapien 37atcctcgtgg gccctgacct tctctctgag agccgggcag aggctccgga gccatgcagg 60ccgaaggccg gggcacaggg ggttcgacgg gcgatgctga tggcccagga ggccctggca 120ttcctgatgg cccagggggc aatgctggcg gcccaggaga ggcgggtgcc acgggcggca 180gaggtccccg gggcgcaggg gcagcaaggg cctcggggcc gggaggaggc gccccgcggg 240gtccgcatgg cggcgcggct tcagggctga atggatgctg cagatgcggg gccagggggc 300cggagagccg cctgcttgag ttctacctcg ccatgccttt cgcgacaccc atggaagcag 360agctggcccg caggagcctg gcccaggatg ccccaccgct tcccgtgcca ggggtgcttc 420tgaaggagtt cactgtgtcc ggcaacatac tgactatccg actgactgct gcagaccacc 480gccaactgca gctctccatc agctcctgtc tccagcagct ttccctgttg atgtggatca 540cgcagtgctt tctgcccgtg tttttggctc agcctccctc agggcagagg cgctaagccc 600agcctggcgc cccttcctag gtcatgcctc ctcccctagg gaatggtccc agcacgagtg 660gccagttcat tgtgggggcc tgattgtttg tcgctggagg aggacggctt acatgtttgt 720ttctgtagaa aataaaactg agctacgaaa aa 752 38 750 PRT Homo Sapien 38 MetTrp Asn Leu Leu His Glu Thr Asp Ser Ala Val Ala Thr Ala Arg 1 5 10 15Arg Pro Arg Trp Leu Cys Ala Gly Ala Leu Val Leu Ala Gly Gly Phe 20 25 30Phe Leu Leu Gly Phe Leu Phe Gly Trp Phe Ile Lys Ser Ser Asn Glu 35 40 45Ala Thr Asn Ile Thr Pro Lys His Asn Met Lys Ala Phe Leu Asp Glu 50 55 60Leu Lys Ala Glu Asn Ile Lys Lys Phe Leu Tyr Asn Phe Thr Gln Ile 65 70 7580 Pro His Leu Ala Gly Thr Glu Gln Asn Phe Gln Leu Ala Lys Gln Ile 85 9095 Gln Ser Gln Trp Lys Glu Phe Gly Leu Asp Ser Val Glu Leu Ala His 100105 110 Tyr Asp Val Leu Leu Ser Tyr Pro Asn Lys Thr His Pro Asn Tyr Ile115 120 125 Ser Ile Ile Asn Glu Asp Gly Asn Glu Ile Phe Asn Thr Ser LeuPhe 130 135 140 Glu Pro Pro Pro Pro Gly Tyr Glu Asn Val Ser Asp Ile ValPro Pro 145 150 155 160 Phe Ser Ala Phe Ser Pro Gln Gly Met Pro Glu GlyAsp Leu Val Tyr 165 170 175 Val Asn Tyr Ala Arg Thr Glu Asp Phe Phe LysLeu Glu Arg Asp Met 180 185 190 Lys Ile Asn Cys Ser Gly Lys Ile Val IleAla Arg Tyr Gly Lys Val 195 200 205 Phe Arg Gly Asn Lys Val Lys Asn AlaGln Leu Ala Gly Ala Lys Gly 210 215 220 Val Ile Leu Tyr Ser Asp Pro AlaAsp Tyr Phe Ala Pro Gly Val Lys 225 230 235 240 Ser Tyr Pro Asp Gly TrpAsn Leu Pro Gly Gly Gly Val Gln Arg Gly 245 250 255 Asn Ile Leu Asn LeuAsn Gly Ala Gly Asp Pro Leu Thr Pro Gly Tyr 260 265 270 Pro Ala Asn GluTyr Ala Tyr Arg Arg Gly Ile Ala Glu Ala Val Gly 275 280 285 Leu Pro SerIle Pro Val His Pro Ile Gly Tyr Tyr Asp Ala Gln Lys 290 295 300 Leu LeuGlu Lys Met Gly Gly Ser Ala Pro Pro Asp Ser Ser Trp Arg 305 310 315 320Gly Ser Leu Lys Val Pro Tyr Asn Val Gly Pro Gly Phe Thr Gly Asn 325 330335 Phe Ser Thr Gln Lys Val Lys Met His Ile His Ser Thr Asn Glu Val 340345 350 Thr Arg Ile Tyr Asn Val Ile Gly Thr Leu Arg Gly Ala Val Glu Pro355 360 365 Asp Arg Tyr Val Ile Leu Gly Gly His Arg Asp Ser Trp Val PheGly 370 375 380 Gly Ile Asp Pro Gln Ser Gly Ala Ala Val Val His Glu IleVal Arg 385 390 395 400 Ser Phe Gly Thr Leu Lys Lys Glu Gly Trp Arg ProArg Arg Thr Ile 405 410 415 Leu Phe Ala Ser Trp Asp Ala Glu Glu Phe GlyLeu Leu Gly Ser Thr 420 425 430 Glu Trp Ala Glu Glu Asn Ser Arg Leu LeuGln Glu Arg Gly Val Ala 435 440 445 Tyr Ile Asn Ala Asp Ser Ser Ile GluGly Asn Tyr Thr Leu Arg Val 450 455 460 Asp Cys Thr Pro Leu Met Tyr SerLeu Val His Asn Leu Thr Lys Glu 465 470 475 480 Leu Lys Ser Pro Asp GluGly Phe Glu Gly Lys Ser Leu Tyr Glu Ser 485 490 495 Trp Thr Lys Lys SerPro Ser Pro Glu Phe Ser Gly Met Pro Arg Ile 500 505 510 Ser Lys Leu GlySer Gly Asn Asp Phe Glu Val Phe Phe Gln Arg Leu 515 520 525 Gly Ile AlaSer Gly Arg Ala Arg Tyr Thr Lys Asn Trp Glu Thr Asn 530 535 540 Lys PheSer Gly Tyr Pro Leu Tyr His Ser Val Tyr Glu Thr Tyr Glu 545 550 555 560Leu Val Glu Lys Phe Tyr Asp Pro Met Phe Lys Tyr His Leu Thr Val 565 570575 Ala Gln Val Arg Gly Gly Met Val Phe Glu Leu Ala Asn Ser Ile Val 580585 590 Leu Pro Phe Asp Cys Arg Asp Tyr Ala Val Val Leu Arg Lys Tyr Ala595 600 605 Asp Lys Ile Tyr Ser Ile Ser Met Lys His Pro Gln Glu Met LysThr 610 615 620 Tyr Ser Val Ser Phe Asp Ser Leu Phe Ser Ala Val Lys AsnPhe Thr 625 630 635 640 Glu Ile Ala Ser Lys Phe Ser Glu Arg Leu Gln AspPhe Asp Lys Ser 645 650 655 Asn Pro Ile Val Leu Arg Met Met Asn Asp GlnLeu Met Phe Leu Glu 660 665 670 Arg Ala Phe Ile Asp Pro Leu Gly Leu ProAsp Arg Pro Phe Tyr Arg 675 680 685 His Val Ile Tyr Ala Pro Ser Ser HisAsn Lys Tyr Ala Gly Glu Ser 690 695 700 Phe Pro Gly Ile Tyr Asp Ala LeuPhe Asp Ile Glu Ser Lys Val Asp 705 710 715 720 Pro Ser Lys Ala Trp GlyGlu Val Lys Arg Gln Ile Tyr Val Ala Ala 725 730 735 Phe Thr Val Gln AlaAla Ala Glu Thr Leu Ser Glu Val Ala 740 745 750 39 2653 DNA Homo Sapien39 ctcaaaaggg gccggatttc cttctcctgg aggcagatgt tgcctctctc tctcgctcgg 60attggttcag tgcactctag aaacactgct gtggtggaga aactggaccc caggtctgga 120gcgaattcca gcctgcaggg ctgataagcg aggcattagt gagattgaga gagactttac 180cccgccgtgg tggttggagg gcgcgcagta gagcagcagc acaggcgcgg gtcccgggag 240gccggctctg ctcgcgccga gatgtggaat ctccttcacg aaaccgactc ggctgtggcc 300accgcgcgcc gcccgcgctg gctgtgcgct ggggcgctgg tgctggcggg tggcttcttt 360ctcctcggct tcctcttcgg gtggtttata aaatcctcca atgaagctac taacattact 420ccaaagcata atatgaaagc atttttggat gaattgaaag ctgagaacat caagaagttc 480ttatataatt ttacacagat accacattta gcaggaacag aacaaaactt tcagcttgca 540aagcaaattc aatcccagtg gaaagaattt ggcctggatt ctgttgagct agcacattat 600gatgtcctgt tgtcctaccc aaataagact catcccaact acatctcaat aattaatgaa 660gatggaaatg agattttcaa cacatcatta tttgaaccac ctcctccagg atatgaaaat 720gtttcggata ttgtaccacc tttcagtgct ttctctcctc aaggaatgcc agagggcgat 780ctagtgtatg ttaactatgc acgaactgaa gacttcttta aattggaacg ggacatgaaa 840atcaattgct ctgggaaaat tgtaattgcc agatatggga aagttttcag aggaaataag 900gttaaaaatg cccagctggc aggggccaaa ggagtcattc tctactccga ccctgctgac 960tactttgctc ctggggtgaa gtcctatcca gatggttgga atcttcctgg aggtggtgtc 1020cagcgtggaa atatcctaaa tctgaatggt gcaggagacc ctctcacacc aggttaccca 1080gcaaatgaat atgcttatag gcgtggaatt gcagaggctg ttggtcttcc aagtattcct 1140gttcatccaa ttggatacta tgatgcacag aagctcctag aaaaaatggg tggctcagca 1200ccaccagata gcagctggag aggaagtctc aaagtgccct acaatgttgg acctggcttt 1260actggaaact tttctacaca aaaagtcaag atgcacatcc actctaccaa tgaagtgaca 1320agaatttaca atgtgatagg tactctcaga ggagcagtgg aaccagacag atatgtcatt 1380ctgggaggtc accgggactc atgggtgttt ggtggtattg accctcagag tggagcagct 1440gttgttcatg aaattgtgag gagctttgga acactgaaaa aggaagggtg gagacctaga 1500agaacaattt tgtttgcaag ctgggatgca gaagaatttg gtcttcttgg ttctactgag 1560tgggcagagg agaattcaag actccttcaa gagcgtggcg tggcttatat taatgctgac 1620tcatctatag aaggaaacta cactctgaga gttgattgta caccgctgat gtacagcttg 1680gtacacaacc taacaaaaga gctgaaaagc cctgatgaag gctttgaagg caaatctctt 1740tatgaaagtt ggactaaaaa aagtccttcc ccagagttca gtggcatgcc caggataagc 1800aaattgggat ctggaaatga ttttgaggtg ttcttccaac gacttggaat tgcttcaggc 1860agagcacggt atactaaaaa ttgggaaaca aacaaattca gcggctatcc actgtatcac 1920agtgtctatg aaacatatga gttggtggaa aagttttatg atccaatgtt taaatatcac 1980ctcactgtgg cccaggttcg aggagggatg gtgtttgagc tagccaattc catagtgctc 2040ccttttgatt gtcgagatta tgctgtagtt ttaagaaagt atgctgacaa aatctacagt 2100atttctatga aacatccaca ggaaatgaag acatacagtg tatcatttga ttcacttttt 2160tctgcagtaa agaattttac agaaattgct tccaagttca gtgagagact ccaggacttt 2220gacaaaagca acccaatagt attaagaatg atgaatgatc aactcatgtt tctggaaaga 2280gcatttattg atccattagg gttaccagac aggccttttt ataggcatgt catctatgct 2340ccaagcagcc acaacaagta tgcaggggag tcattcccag gaatttatga tgctctgttt 2400gatattgaaa gcaaagtgga cccttccaag gcctggggag aagtgaagag acagatttat 2460gttgcagcct tcacagtgca ggcagctgca gagactttga gtgaagtagc ctaagaggat 2520tctttagaga atccgtattg aatttgtgtg gtatgtcact cagaaagaat cgtaatgggt 2580atattgataa attttaaaat tggtatattt gaaataaagt tgaatattat atataaaaaa 2640aaaaaaaaaa aaa 2653 40 188 PRT Homo Sapien 40 Met Asn Gly Asp Asp AlaPhe Ala Arg Arg Pro Thr Val Gly Ala Gln 1 5 10 15 Ile Pro Glu Lys IleGln Lys Ala Phe Asp Asp Ile Ala Lys Tyr Phe 20 25 30 Ser Lys Glu Glu TrpGlu Lys Met Lys Ala Ser Glu Lys Ile Phe Tyr 35 40 45 Val Tyr Met Lys ArgLys Tyr Glu Ala Met Thr Lys Leu Gly Phe Lys 50 55 60 Ala Thr Leu Pro ProPhe Met Cys Asn Lys Arg Ala Glu Asp Phe Gln 65 70 75 80 Gly Asn Asp LeuAsp Asn Asp Pro Asn Arg Gly Asn Gln Val Glu Arg 85 90 95 Pro Gln Met ThrPhe Gly Arg Leu Gln Gly Ile Ser Pro Lys Ile Met 100 105 110 Pro Lys LysPro Ala Glu Glu Gly Asn Asp Ser Glu Glu Val Pro Glu 115 120 125 Ala SerGly Pro Gln Asn Asp Gly Lys Glu Leu Cys Pro Pro Gly Lys 130 135 140 ProThr Thr Ser Glu Lys Ile His Glu Arg Ser Gly Pro Lys Arg Gly 145 150 155160 Glu His Ala Trp Thr His Arg Leu Arg Glu Arg Lys Gln Leu Val Ile 165170 175 Tyr Glu Glu Ile Ser Asp Pro Glu Glu Asp Asp Glu 180 185 41 766DNA Homo Sapien 41 ctctctttcg attcttccat actcagagta cgcacggtctgattttctct ttggattctt 60 ccaaaatcag agtcagactg ctcccggtgc catgaacggagacgacgcct ttgcaaggag 120 acccacggtt ggtgctcaaa taccagagaa gatccaaaaggccttcgatg atattgccaa 180 atacttctct aaggaagagt gggaaaagat gaaagcctcggagaaaatct tctatgtgta 240 tatgaagaga aagtatgagg ctatgactaa actaggtttcaaggccaccc tcccaccttt 300 catgtgtaat aaacgggccg aagacttcca ggggaatgatttggataatg accctaaccg 360 tgggaatcag gttgaacgtc ctcagatgac tttcggcaggctccagggaa tctccccgaa 420 gatcatgccc aagaagccag cagaggaagg aaatgattcggaggaagtgc cagaagcatc 480 tggcccacaa aatgatggga aagagctgtg ccccccgggaaaaccaacta cctctgagaa 540 gattcacgag agatctggac ccaaaagggg ggaacatgcctggacccaca gactgcgtga 600 gagaaaacag ctggtgattt atgaagagat cagcgaccctgaggaagatg acgagtaact 660 cccctcaggg atacgacaca tgcccatgat gagaagcagaacgtggtgac ctttcacgaa 720 catgggcatg gctgcggacc cctcgtcatc aggtgcatagcaagtg 766 42 903 DNA Herpes Simplex Virus 42 atgacctctc gccgctccgtgaagtcgggt ccgcgggagg ttccgcgcga tgagtacgag 60 gatctgtact acaccccgtcttcaggtatg gcgagtcccg atagtccgcc tgacacctcc 120 cgccgtggcg ccctacagacacgctcgcgc cagaggggcg aggtccgttt cgtccagtac 180 gacgagtcgg attatgccctctacgggggc tcgtcatccg aagacgacga acacccggag 240 gtcccccgga cgcggcgtcccgtttccggg gcggttttgt ccggcccggg gcctgcgcgg 300 gcgcctccgc cacccgctgggtccggaggg gccggacgca cacccaccac cgccccccgg 360 gccccccgaa cccagcgggtggcgactaag gcccccgcgg ccccggcggc ggagaccacc 420 cgcggcagga aatcggcccagccagaatcc gccgcactcc cagacgcccc cgcgtcgacg 480 gcgccaaccc gatccaagacacccgcgcag gggctggcca gaaagctgca ctttagcacc 540 gcccccccaa accccgacgcgccatggacc ccccgggtgg ccggctttaa caagcgcgtc 600 ttctgcgccg cggtcgggcgcctggcggcc atgcatgccc ggatggcggc ggtccagctc 660 tgggacatgt cgcgtccgcgcacagacgaa gacctcaacg aactccttgg catcaccacc 720 atccgcgtga cggtctgcgagggcaaaaac ctgcttcagc gcgccaacga gttggtgaat 780 ccagacgtgg tgcaggacgtcgacgcggcc acggcgactc gagggcgttc tgcggcgtcg 840 cgccccaccg agcgacctcgagccccagcc cgctccgctt ctcgccccag acggcccgtc 900 gag 903 43 311 PRTHerpes Simplex Virus 43 Met Thr Ser Arg Arg Ser Val Lys Ser Gly Pro ArgGlu Val Pro Arg 1 5 10 15 Asp Glu Tyr Glu Asp Leu Tyr Tyr Thr Pro SerSer Gly Met Ala Ser 20 25 30 Pro Asp Ser Pro Pro Asp Thr Ser Arg Arg GlyAla Leu Phe Thr Gln 35 40 45 Thr Arg Ser Arg Gln Arg Gly Glu Val Arg PheVal Gln Tyr Asp Glu 50 55 60 Ser Asp Tyr Ala Leu Tyr Gly Gly Ser Ser SerGlu Asp Asp Glu His 65 70 75 80 Pro Glu Val Pro Arg Thr Arg Arg Pro ValSer Gly Ala Val Leu Ser 85 90 95 Gly Pro Gly Pro Ala Arg Ala Pro Pro ProPhe Thr Pro Ala Gly Ser 100 105 110 Gly Gly Ala Gly Arg Thr Pro Thr ThrAla Pro Arg Ala Pro Arg Thr 115 120 125 Gln Arg Val Ala Thr Lys Ala ProAla Ala Pro Ala Ala Glu Thr Thr 130 135 140 Arg Gly Arg Lys Ser Ala GlnPro Glu Ser Ala Ala Leu Pro Asp Ala 145 150 155 160 Pro Ala Ser Thr AlaPro Thr Phe Thr Arg Ser Lys Thr Pro Ala Gln 165 170 175 Gly Leu Ala ArgLys Leu His Phe Ser Thr Ala Pro Pro Asn Pro Asp 180 185 190 Ala Pro TrpThr Pro Arg Val Ala Gly Phe Asn Lys Arg Val Phe Cys 195 200 205 Ala AlaVal Gly Arg Leu Ala Ala Met His Ala Arg Met Ala Ala Val 210 215 220 GlnLeu Trp Asp Phe Thr Met Ser Arg Pro Arg Thr Asp Glu Asp Leu 225 230 235240 Asn Glu Leu Leu Gly Ile Thr Thr Ile Arg Val Thr Val Cys Glu Gly 245250 255 Lys Asn Leu Leu Gln Arg Ala Asn Glu Leu Val Asn Pro Asp Val Val260 265 270 Gln Asp Val Asp Ala Ala Thr Ala Thr Arg Gly Arg Ser Ala AlaSer 275 280 285 Arg Phe Thr Pro Thr Glu Arg Pro Arg Ala Pro Ala Arg SerAla Ser 290 295 300 Arg Pro Arg Arg Pro Val Glu 305 310 44 9 PRTAdenovirus 3 44 Leu Ile Val Ile Gly Ile Leu Ile Leu 1 5 45 10 PRTAdenovirus 5 45 Ser Gly Pro Ser Asn Thr Pro Pro Glu Ile 1 5 10 46 8 PRTAdenovirus 5 46 Val Asn Ile Arg Asn Cys Cys Tyr 1 5 47 10 PRT Adenovirus5 47 Ser Gly Pro Ser Asn Ile Pro Pro Glu Ile 1 5 10 48 9 PRT ClassicalSwine Fever Virus 48 Glu Asn Ala Leu Leu Val Ala Leu Phe 1 5 49 9 PRTDengue Virus 4 49 Thr Pro Glu Gly Ile Ile Pro Thr Leu 1 5 50 9 PRTEpstein-Barr Virus 50 Cys Leu Gly Gly Leu Leu Thr Met Val 1 5 51 9 PRTEpstein-Barr Virus 51 Asn Ile Ala Glu Gly Leu Arg Ala Leu 1 5 52 9 PRTEpstein-Barr Virus 52 Asn Leu Arg Arg Gly Thr Ala Leu Ala 1 5 53 9 PRTEpstein-Barr Virus 53 Ala Leu Ala Ile Pro Gln Cys Arg Leu 1 5 54 9 PRTEpstein-Barr Virus 54 Val Leu Lys Asp Ala Ile Lys Asp Leu 1 5 55 9 PRTEpstein-Barr Virus 55 Phe Met Val Phe Leu Gln Thr His Ile 1 5 56 9 PRTEpstein-Barr Virus 56 His Leu Ile Val Asp Thr Asp Ser Leu 1 5 57 9 PRTEpstein-Barr Virus 57 Ser Leu Gly Asn Pro Ser Leu Ser Val 1 5 58 9 PRTEpstein-Barr Virus 58 Pro Leu Ala Ser Ala Met Arg Met Leu 1 5 59 8 PRTEpstein-Barr Virus 59 Arg Met Leu Trp Met Ala Asn Tyr 1 5 60 9 PRTEpstein-Barr Virus 60 Met Leu Trp Met Ala Asn Tyr Ile Val 1 5 61 9 PRTEpstein-Barr Virus 61 Ile Leu Pro Gln Gly Pro Gln Thr Ala 1 5 62 9 PRTEpstein-Barr Virus 62 Pro Leu Arg Pro Thr Ala Pro Thr Ile 1 5 63 9 PRTEpstein-Barr Virus 63 Pro Leu Pro Pro Ala Thr Leu Thr Val 1 5 64 9 PRTEpstein-Barr Virus 64 Arg Met His Leu Pro Val Leu His Val 1 5 65 9 PRTEpstein-Barr Virus 65 Pro Met Pro Leu Pro Pro Ser Gln Leu 1 5 66 9 PRTEpstein-Barr Virus 66 Gln Leu Pro Pro Pro Ala Ala Pro Ala 1 5 67 9 PRTEpstein-Barr Virus 67 Ser Met Pro Glu Leu Ser Pro Val Leu 1 5 68 9 PRTEpstein-Barr Virus 68 Asp Leu Asp Glu Ser Trp Asp Tyr Ile 1 5 69 9 PRTEpstein-Barr Virus 69 Pro Leu Pro Cys Val Leu Trp Pro Val 1 5 70 9 PRTEpstein-Barr Virus 70 Ser Leu Glu Glu Cys Asp Ser Glu Leu 1 5 71 9 PRTEpstein-Barr Virus 71 Glu Ile Lys Arg Tyr Lys Asn Arg Val 1 5 72 9 PRTEpstein-Barr Virus 72 Gln Leu Leu Gln His Tyr Arg Glu Val 1 5 73 9 PRTEpstein-Barr Virus 73 Leu Leu Gln His Tyr Arg Glu Val Ala 1 5 74 9 PRTEpstein-Barr Virus 74 Leu Leu Lys Gln Met Cys Pro Ser Leu 1 5 75 9 PRTEpstein-Barr Virus 75 Ser Ile Ile Pro Arg Thr Pro Asp Val 1 5 76 10 PRTEpstein-Barr Virus 76 Leu Leu Asp Phe Val Arg Phe Met Gly Val 1 5 10 779 PRT Epstein-Barr Virus 77 Ser Val Arg Asp Arg Leu Ala Arg Leu 1 5 78 9PRT Epstein-Barr Virus 78 Ile Val Thr Asp Phe Ser Val Ile Lys 1 5 79 10PRT Epstein-Barr Virus 79 Ala Val Phe Asp Arg Lys Ser Asp Ala Lys 1 5 1080 8 PRT Epstein-Barr Virus 80 Arg Tyr Ser Ile Phe Phe Asp Tyr 1 5 81 9PRT Epstein-Barr Virus 81 Gln Pro Arg Ala Pro Ile Arg Pro Ile 1 5 82 9PRT Epstein-Barr Virus 82 Arg Pro Pro Ile Phe Ile Arg Arg Ile 1 5 83 9PRT Epstein-Barr Virus 83 Glu Pro Asp Val Pro Pro Gly Ala Ile 1 5 84 9PRT Epstein-Barr Virus 84 Ile Pro Gln Cys Arg Leu Thr Pro Leu 1 5 85 9PRT Epstein-Barr Virus 85 Gly Pro Gly Pro Gln Pro Gly Pro Leu 1 5 86 9PRT Epstein-Barr Virus 86 Gln Pro Gly Pro Leu Arg Glu Ser Ile 1 5 87 9PRT Epstein-Barr Virus 87 Arg Pro Gln Lys Arg Pro Ser Cys Ile 1 5 88 9PRT Epstein-Barr Virus 88 Pro Pro Thr Pro Leu Leu Thr Val Leu 1 5 89 9PRT Epstein-Barr Virus 89 Thr Pro Ser Pro Pro Arg Met His Leu 1 5 90 9PRT Epstein-Barr Virus 90 Pro Pro Arg Met His Leu Pro Val Leu 1 5 91 9PRT Epstein-Barr Virus 91 Val Pro Asp Gln Ser Met His Pro Leu 1 5 92 9PRT Epstein-Barr Virus 92 Pro Pro Ser Ile Asp Pro Ala Asp Leu 1 5 93 9PRT Epstein-Barr Virus 93 Leu Pro Cys Val Leu Trp Pro Val Leu 1 5 94 10PRT Epstein-Barr Virus 94 Cys Pro Ser Leu Asp Val Asp Ser Ile Ile 1 5 1095 9 PRT Epstein-Barr Virus 95 Thr Pro Asp Val Leu His Glu Asp Leu 1 596 9 PRT Epstein-Barr Virus 96 Phe Leu Arg Gly Arg Ala Tyr Gly Leu 1 597 9 PRT Epstein-Barr Virus 97 Gln Ala Lys Trp Arg Leu Gln Thr Leu 1 598 9 PRT Epstein-Barr Virus 98 Ala Tyr Pro Leu His Glu Gln His Gly 1 599 9 PRT Epstein-Barr Virus 99 Tyr Leu Lys Ser Phe Val Ser Asp Ala 1 5100 9 PRT Epstein-Barr Virus 100 Arg Arg Arg Trp Arg Arg Leu Thr Val 1 5101 9 PRT Epstein-Barr Virus 101 Arg Arg Ile Tyr Asp Leu Ile Glu Leu 1 5102 9 PRT Epstein-Barr Virus 102 Tyr Pro Leu His Glu Gln His Gly Met 1 5103 9 PRT Epstein-Barr Virus 103 Tyr Pro Leu His Glu Gln His Gly Met 1 5104 9 PRT Hepatitis C Virus 104 His Ser Lys Lys Lys Cys Asp Glu Leu 1 5105 8 PRT Hepatitis C Virus 105 Ala Ser Arg Cys Trp Val Ala Met 1 5 1069 PRT Hepatitis C Virus 106 Gly Gln Ile Val Gly Gly Val Tyr Leu 1 5 10710 PRT Hepatitis C Virus 107 Pro Pro Leu Thr Asp Phe Asp Gln Gly Trp 1 510 108 10 PRT Hepatitis C Virus 108 Leu Met Gly Tyr Ile Pro Leu Val GlyAla 1 5 10 109 10 PRT Hepatitis C Virus 109 Ala Asp Leu Met Gly Tyr IlePro Leu Val 1 5 10 110 16 PRT Hepatitis C Virus 110 Met Ser Tyr Ser TrpThr Gly Ala Leu Val Thr Pro Cys Ala Glu Glu 1 5 10 15 111 9 PRTHepatitis C Virus 111 Lys His Pro Asp Ala Thr Tyr Ser Arg 1 5 112 10 PRTHepatitis C Virus 1 112 Lys Leu Val Ala Leu Gly Ile Asn Ala Val 1 5 10113 9 PRT Hepatitis C Virus 1 113 Gly Asp Phe Asp Ser Val Ile Asp Cys 15 114 9 PRT Hepatitis C Virus 1 114 Gly Asn Ala Ser Arg Cys Trp Val Ala1 5 115 9 PRT Hepatitis C Virus 1 115 Thr Arg Pro Pro Leu Gly Asn TrpPhe 1 5 116 9 PRT Hepatitis C Virus 1 116 Val Pro His Pro Asn Ile GluGlu Val 1 5 117 9 PRT Hepatitis C Virus 1 117 Tyr Thr Gly Asp Phe AspSer Val Ile 1 5 118 8 PRT Hepatitis C Virus 1 118 Ser Trp Ala Ile LysTrp Glu Tyr 1 5 119 9 PRT Hepatitis C Virus 1 119 Lys His Pro Asp AlaThr Tyr Ser Arg 1 5 120 9 PRT Hepatitis C Virus 1 120 Gly Asp Phe AspSer Val Ile Asp Cys 1 5 121 9 PRT Human Immunodeficiency Virus 121 ArgTyr Leu Lys Asp Gln Gln Leu Leu 1 5 122 9 PRT Human ImmunodeficiencyVirus 122 Ile Val Gly Leu Asn Lys Ile Val Arg 1 5 123 9 PRT HumanImmunodeficiency Virus 123 Glu Ile Tyr Lys Arg Trp Ile Ile Leu 1 5 124 8PRT Human Immunodeficiency Virus 124 Gly Glu Leu Tyr Lys Arg Trp Ile 1 5125 9 PRT Human Immunodeficiency Virus 125 Glu Ile Lys Asp Thr Lys GluAla Leu 1 5 126 8 PRT Human Immunodeficiency Virus 126 Tyr Leu Lys AspGln Gln Leu Leu 1 5 127 11 PRT Human Immunodeficiency Virus 127 Ile LeuGly Leu Asn Lys Ile Val Arg Met Tyr 1 5 10 128 9 PRT HumanImmunodeficiency Virus 128 Glu Arg Tyr Leu Lys Asp Gln Gln Leu 1 5 12911 PRT Human Immunodeficiency Virus 129 Tyr His Thr Gln Gly Tyr Phe ProGln Trp Gln 1 5 10 130 12 PRT Human Immunodeficiency Virus 130 Thr GlnGly Tyr Phe Pro Gln Trp Gln Asn Tyr Thr 1 5 10 131 9 PRT HumanImmunodeficiency Virus 131 Gly Arg Ala Phe Val Thr Leu Gly Lys 1 5 132 9PRT Human Immunodeficiency Virus 132 Lys Arg Trp Ile Ile Leu Gly Leu Asn1 5 133 10 PRT Human Immunodeficiency Virus 133 Gln Val Pro Leu Arg ProMet Thr Tyr Lys 1 5 10 134 9 PRT Human Immunodeficiency Virus 134 ThrGln Gly Tyr Phe Pro Gln Trp Gln 1 5 135 9 PRT Human ImmunodeficiencyVirus 135 His Gln Ala Ile Ser Pro Arg Thr Ile 1 5 136 12 PRT HumanImmunodeficiency Virus 136 Gln Met Val His Gln Ala Ile Ser Pro Arg ThrLeu 1 5 10 137 10 PRT Human Immunodeficiency Virus 137 Met Tyr Ala ProPro Ile Gly Gly Gln Ile 1 5 10 138 10 PRT Human Immunodeficiency Virus138 Arg Gly Pro Gly Arg Ala Phe Val Thr Ile 1 5 10 139 9 PRT HumanImmunodeficiency Virus 139 Met Pro Gly Arg Ala Phe Val Thr Ile 1 5 140 9PRT Human Immunodeficiency Virus 1 140 Ile Leu Lys Glu Pro Val His GlyVal 1 5 141 9 PRT Human Immunodeficiency Virus 1 141 Ala Phe His His ValAla Arg Glu Leu 1 5 142 9 PRT Human Immunodeficiency Virus 1 142 Lys LeuThr Pro Leu Cys Val Thr Leu 1 5 143 10 PRT Human Immunodeficiency Virus1 143 Ser Leu Leu Asn Ala Thr Asp Ile Ala Val 1 5 10 144 9 PRT HumanImmunodeficiency Virus 1 144 Val Ile Tyr Gln Tyr Met Asp Asp Leu 1 5 1459 PRT Human Immunodeficiency Virus 1 145 Ser Leu Tyr Asn Thr Val Ala ThrLeu 1 5 146 9 PRT Human Immunodeficiency Virus 1 146 Arg Gly Pro Gly ArgAla Phe Val Thr 1 5 147 11 PRT Human Immunodeficiency Virus 1 147 ArgLeu Arg Asp Leu Leu Leu Ile Val Thr Arg 1 5 10 148 10 PRT HumanImmunodeficiency Virus 1 148 Gln Val Pro Leu Arg Pro Met Thr Tyr Lys 1 510 149 10 PRT Human Immunodeficiency Virus 1 149 Thr Val Tyr Tyr Gly ValPro Val Trp Lys 1 5 10 150 9 PRT Human Immunodeficiency Virus 1 150 ArgLeu Arg Pro Gly Gly Lys Lys Lys 1 5 151 9 PRT Human ImmunodeficiencyVirus 1 151 Val Tyr Tyr Gly Val Pro Val Trp Lys 1 5 152 9 PRT HumanImmunodeficiency Virus 1 152 Val Pro Leu Arg Pro Met Thr Tyr Lys 1 5 1539 PRT Human Immunodeficiency Virus 1 153 Ala Ile Phe Gln Ser Ser Met ThrLys 1 5 154 10 PRT Human Immunodeficiency Virus 1 154 Gln Val Pro LeuArg Pro Met Thr Tyr Lys 1 5 10 155 12 PRT Human Immunodeficiency Virus 1155 Ala Ala Val Asp Leu Ser His Phe Leu Lys Glu Lys 1 5 10 156 12 PRTHuman Immunodeficiency Virus 1 156 Ala Cys Gln Gly Val Gly Gly Pro GlyGly His Lys 1 5 10 157 10 PRT Human Immunodeficiency Virus 1 157 Glu ThrIle Asn Glu Glu Ala Ala Glu Trp 1 5 10 158 10 PRT Human ImmunodeficiencyVirus 1 158 Thr Pro Gly Pro Gly Val Arg Tyr Pro Leu 1 5 10 159 8 PRTHuman Immunodeficiency Virus 1 159 Gly Gly Lys Lys Lys Tyr Lys Leu 1 5160 9 PRT Human Immunodeficiency Virus 1 160 Arg Val Lys Glu Lys Tyr GlnHis Leu 1 5 161 9 PRT Human Immunodeficiency Virus 1 161 Asp Arg Phe TyrLys Thr Leu Arg Ala 1 5 162 16 PRT Human Immunodeficiency Virus 1 162Gly Val Arg Tyr Pro Leu Thr Phe Gly Trp Cys Tyr Lys Leu Val Pro 1 5 1015 163 10 PRT Human Immunodeficiency Virus 1 163 Lys Arg Trp Ile Ile LeuGly Leu Asn Lys 1 5 10 164 9 PRT Human Immunodeficiency Virus 1 164 AlaPhe His His Val Ala Arg Glu Leu 1 5 165 9 PRT Epstein-Barr Virus 165 LysGlu His Val Ile Gln Asn Ala Phe 1 5 166 10 PRT Epstein-Barr Virus 166Glu Glu Asn Leu Leu Asp Phe Val Arg Phe 1 5 10 167 10 PRT Epstein-BarrVirus 167 Asp Thr Pro Leu Ile Pro Leu Thr Ile Phe 1 5 10 168 10 PRTEpstein-Barr Virus 168 Gln Asn Gly Ala Leu Ala Ile Asn Thr Phe 1 5 10169 9 PRT Epstein-Barr Virus 169 Arg Leu Arg Ala Glu Ala Gly Val Lys 1 5170 10 PRT Hepatitis B Virus 170 Gly Leu Ser Pro Thr Val Trp Leu Ser Val1 5 10 171 9 PRT Hepatitis B Virus 171 Trp Leu Ser Leu Leu Val Pro PheVal 1 5 172 10 PRT Hepatitis B Virus 172 Phe Leu Pro Ser Asp Phe Phe ProSer Val 1 5 10 173 10 PRT Hepatitis B Virus 173 Phe Leu Pro Ser Asp PhePhe Pro Ser Val 1 5 10 174 10 PRT Hepatitis B Virus 174 Phe Leu Pro SerAsp Phe Phe Pro Ser Val 1 5 10 175 10 PRT Hepatitis B Virus 175 Phe LeuPro Ser Asp Phe Phe Pro Ser Val 1 5 10 176 9 PRT Hepatitis B Virus 176Phe Leu Leu Ser Leu Gly Ile His Leu 1 5 177 9 PRT Hepatitis B Virus 177Ser Leu Tyr Ala Asp Ser Pro Ser Val 1 5 178 9 PRT Hepatitis B Virus 178Gly Leu Ser Arg Tyr Val Ala Arg Leu 1 5 179 10 PRT Hepatitis B Virus 179Leu Leu Val Pro Phe Val Gln Trp Phe Val 1 5 10 180 9 PRT Hepatitis BVirus 180 Ala Leu Met Pro Leu Tyr Ala Cys Ile 1 5 181 10 PRT Hepatitis BVirus 181 Leu Leu Pro Ile Phe Phe Cys Leu Trp Val 1 5 10 182 9 PRTHepatitis B Virus 182 Tyr Met Asp Asp Val Val Leu Gly Ala 1 5 183 9 PRTHepatitis B Virus 183 Leu Leu Leu Cys Leu Ile Phe Leu Leu 1 5 184 10 PRTHepatitis B Virus 184 Leu Leu Asp Tyr Gln Gly Met Leu Pro Val 1 5 10 18510 PRT Hepatitis B Virus 185 Ser Ile Val Ser Pro Phe Ile Pro Leu Leu 1 510 186 9 PRT Hepatitis B Virus 186 Phe Leu Leu Thr Arg Ile Leu Thr Ile 15 187 9 PRT Hepatitis B Virus 187 Tyr Val Asn Val Asn Met Gly Leu Lys 15 188 11 PRT Hepatitis B Virus 188 Ser Thr Leu Pro Glu Thr Thr Val ValArg Arg 1 5 10 189 11 PRT Hepatitis B Virus 189 Ser Thr Leu Pro Glu ThrThr Val Val Arg Arg 1 5 10 190 10 PRT Hepatitis B Virus 190 Phe Leu ProSer Asp Phe Phe Pro Ser Val 1 5 10 191 12 PRT Hepatitis B Virus 191 IlePro Gln Ser Leu Asp Ser Trp Trp Thr Ser Leu 1 5 10 192 8 PRT Hepatitis BVirus 192 Met Gly Leu Lys Phe Arg Gln Leu 1 5 193 9 PRT Hepatitis BVirus VARIANT 4, 8 Xaa = Any Amino Acid 193 Ser Thr Asx Xaa Gln Ser GlyXaa Gln 1 5 194 11 PRT Human Cytomegalovirus 194 Phe Ile Ala Gly Asn SerAla Tyr Glu Tyr Val 1 5 10 195 12 PRT Human Cytomegalovirus 195 Ser AspGlu Glu Phe Ala Ile Val Ala Tyr Thr Leu 1 5 10 196 15 PRT HumanCytomegalovirus 196 Asp Asp Val Trp Thr Ser Gly Ser Asp Ser Asp Glu GluLeu Val 1 5 10 15 197 9 PRT Human Cytomegalovirus 197 Ile Pro Ser IleAsn Val His His Tyr 1 5 198 9 PRT Human Cytomegalovirus 198 Asn Leu ValPro Met Val Ala Thr Val 1 5 199 9 PRT Human Cytomegalovirus 199 Asp LeuMet Gly Tyr Ile Pro Leu Val 1 5 200 9 PRT Hepatitis C Virus 200 Asp LeuMet Gly Tyr Ile Pro Leu Val 1 5 201 10 PRT Hepatitis C Virus 201 Leu LeuAla Leu Leu Ser Cys Leu Thr Val 1 5 10 202 8 PRT Hepatitis C Virus 202Ile Leu His Thr Pro Gly Cys Val 1 5 203 10 PRT Hepatitis C Virus 203 GlnLeu Arg Arg His Ile Asp Leu Leu Val 1 5 10 204 9 PRT Hepatitis C Virus204 Asp Leu Cys Gly Ser Val Phe Leu Val 1 5 205 9 PRT Hepatitis C Virus205 Ser Met Val Gly Asn Trp Ala Lys Val 1 5 206 10 PRT Hepatitis C Virus206 His Leu Ile Ile Gln Asn Ile Val Asp Val 1 5 10 207 9 PRT Hepatitis CVirus 207 Phe Leu Leu Leu Ala Asp Ala Arg Val 1 5 208 13 PRT Hepatitis CVirus 208 Gly Leu Arg Asp Leu Ala Val Ala Val Glu Pro Val Val 1 5 10 20911 PRT Hepatitis C Virus 209 Ser Leu Leu Ala Pro Gly Ala Lys Gln Asn Val1 5 10 210 10 PRT Hepatitis C Virus 210 Leu Leu Ala Pro Gly Ala Lys GlnAsn Val 1 5 10 211 10 PRT Hepatitis C Virus 211 Leu Leu Phe Asn Ile LeuGly Gly Trp Val 1 5 10 212 9 PRT Hepatitis C Virus 212 Tyr Leu Val AlaTyr Gln Ala Thr Val 1 5 213 10 PRT Hepatitis C Virus 213 Tyr Leu Leu ProArg Arg Gly Pro Arg Leu 1 5 10 214 10 PRT Hepatitis C Virus 214 Leu LeuAla Leu Leu Ser Cys Leu Thr Ile 1 5 10 215 9 PRT Hepatitis C Virus 215Ser Leu Met Ala Phe Thr Ala Ala Val 1 5 216 9 PRT Hepatitis C Virus 216Cys Ile Asn Gly Val Cys Trp Thr Val 1 5 217 9 PRT Hepatitis C Virus 217Leu Leu Cys Pro Ala Gly His Ala Val 1 5 218 9 PRT Hepatitis C Virus 218Ile Leu Asp Ser Phe Asp Pro Leu Val 1 5 219 9 PRT Hepatitis C Virus 219Ile Leu Ala Gly Tyr Gly Ala Gly Val 1 5 220 9 PRT Hepatitis C Virus 220Gly Leu Gln Asp Cys Thr Met Leu Val 1 5 221 10 PRT Hepatitis C Virus 221Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr 1 5 10 222 9 PRT Hepatitis CVirus 222 His Met Trp Asn Phe Ile Ser Gly Ile 1 5 223 9 PRT Hepatitis CVirus 223 Arg Val Cys Glu Lys Met Ala Leu Tyr 1 5 224 8 PRT Hepatitis CVirus 224 Thr Ile Asn Tyr Thr Ile Phe Lys 1 5 225 8 PRT Hepatitis CVirus 225 Tyr Ile Ser Trp Cys Leu Trp Trp 1 5 226 9 PRT Hepatitis CVirus 226 Gly Pro Arg Leu Gly Val Arg Ala Thr 1 5 227 9 PRT HumanImmunodeficiency Virus 1 227 Ser Phe Asn Cys Gly Gly Glu Phe Phe 1 5 2289 PRT Human Immunodeficiency Virus 1 228 Thr Glu Met Glu Lys Glu Gly LysIle 1 5 229 9 PRT Human Immunodeficiency Virus 1 229 Lys Ile Arg Leu ArgPro Gly Gly Lys 1 5 230 10 PRT Human Immunodeficiency Virus 1 230 ArgLeu Arg Pro Gly Gly Lys Lys Lys Tyr 1 5 10 231 9 PRT HumanImmunodeficiency Virus 1 231 Ala Ile Phe Gln Ser Ser Met Thr Lys 1 5 2329 PRT Human Immunodeficiency Virus 1 232 Thr Leu Tyr Cys Val His Gln ArgIle 1 5 233 10 PRT Human Immunodeficiency Virus 1 233 Ile Tyr Gln GluPro Phe Lys Asn Leu Lys 1 5 10 234 9 PRT Human Immunodeficiency Virus 1234 Lys Tyr Lys Leu Lys His Ile Val Trp 1 5 235 10 PRT HumanImmunodeficiency Virus 1 235 Leu Phe Cys Ala Ser Asp Ala Lys Ala Tyr 1 510 236 11 PRT Human Immunodeficiency Virus 1 236 Gln Ala Ile Ser Pro ArgThr Leu Asn Ala Trp 1 5 10 237 9 PRT Human Immunodeficiency Virus 1 237Glu Val Ile Pro Met Phe Ser Ala Leu 1 5 238 11 PRT HumanImmunodeficiency Virus 1 238 Glu Thr Phe Tyr Val Asp Gly Ala Ala Asn Arg1 5 10 239 11 PRT Human Immunodeficiency Virus 1 239 Arg Leu Arg Asp LeuLeu Leu Ile Val Thr Arg 1 5 10 240 10 PRT Human Immunodeficiency Virus 1240 Pro Ile Gln Lys Glu Thr Trp Glu Thr Trp 1 5 10 241 9 PRT HumanImmunodeficiency Virus 1 241 Arg Ile Lys Gln Ile Ile Asn Met Trp 1 5 2429 PRT Human Immunodeficiency Virus 1 242 Ile Thr Leu Trp Gln Arg Pro LeuVal 1 5 243 9 PRT Human Immunodeficiency Virus 1 243 Asp Thr Val Leu GluGlu Met Asn Leu 1 5 244 9 PRT Human Immunodeficiency Virus 1 244 Ile ThrLeu Trp Gln Arg Pro Leu Val 1 5 245 9 PRT Human Immunodeficiency Virus 1245 Ser Pro Arg Thr Leu Asn Ala Trp Val 1 5 246 9 PRT HumanImmunodeficiency Virus 1 246 Ala Thr Pro Gln Asp Leu Asn Thr Met 1 5 24710 PRT Human Immunodeficiency Virus 1 247 Arg Pro Asn Asn Asn Thr ArgLys Ser Ile 1 5 10 248 9 PRT Human Immunodeficiency Virus 1 248 Ile ProArg Arg Ile Arg Gln Gly Leu 1 5 249 9 PRT Human Immunodeficiency Virus 1249 Glu Leu Arg Ser Leu Tyr Asn Thr Val 1 5 250 8 PRT HumanImmunodeficiency Virus 1 250 Trp Pro Thr Val Arg Glu Arg Met 1 5 251 8PRT Human Immunodeficiency Virus 1 251 Phe Leu Lys Glu Lys Gly Gly Leu 15 252 9 PRT Human Immunodeficiency Virus 1 252 Asp Leu Asn Thr Met LeuAsn Thr Val 1 5 253 10 PRT Human Immunodeficiency Virus 1 253 Lys IleArg Leu Arg Pro Gly Gly Lys Lys 1 5 10 254 9 PRT Human ImmunodeficiencyVirus 1 254 Ile Arg Leu Arg Pro Gly Gly Lys Lys 1 5 255 10 PRT HumanImmunodeficiency Virus 1 255 Gly Arg Arg Gly Trp Glu Ala Leu Lys Tyr 1 510 256 10 PRT Human Immunodeficiency Virus 1 256 Gln Val Pro Leu Arg ProMet Thr Tyr Lys 1 5 10 257 8 PRT Human Immunodeficiency Virus 1 257 ArgTyr Leu Lys Asp Gln Gln Leu 1 5 258 10 PRT Human Immunodeficiency Virus1 258 Arg Arg Gln Asp Ile Leu Asp Leu Trp Ile 1 5 10 259 8 PRT HumanImmunodeficiency Virus 1 259 Arg Tyr Pro Leu Thr Phe Gly Trp 1 5 260 9PRT Human Immunodeficiency Virus 1 260 Trp Ala Ser Arg Glu Leu Glu ArgPhe 1 5 261 9 PRT Human Immunodeficiency Virus 1 261 Thr Val Leu Asp ValGly Asp Ala Tyr 1 5 262 11 PRT Human Immunodeficiency Virus 1 262 ValPro Val Trp Lys Glu Ala Thr Thr Thr Leu 1 5 10 263 9 PRT HumanImmunodeficiency Virus 1 263 Asn Ser Ser Lys Val Ser Gln Asn Tyr 1 5 2649 PRT Human Immunodeficiency Virus 1 264 Pro Pro Ile Pro Val Gly Asp IleTyr 1 5 265 9 PRT Human Immunodeficiency Virus 1 265 His Pro Asp Ile ValIle Tyr Gln Tyr 1 5 266 9 PRT Human Immunodeficiency Virus 1 266 Thr AlaVal Pro Trp Asn Ala Ser Trp 1 5 267 9 PRT Human Immunodeficiency Virus 1267 Asn Pro Val Pro Val Gly Asn Leu Tyr 1 5 268 9 PRT HumanImmunodeficiency Virus 1 268 Tyr Phe Pro Asp Trp Gln Asn Tyr Thr 1 5 2699 PRT Human Immunodeficiency Virus 1 269 Gly His Gln Ala Ala Met Gln MetLeu 1 5 270 10 PRT Human Immunodeficiency Virus 1 270 Arg Leu Arg ProGly Gly Lys Lys Lys Tyr 1 5 10 271 9 PRT Human Immunodeficiency Virus 1271 Tyr Pro Gly Ile Lys Val Arg Gln Leu 1 5 272 10 PRT HumanImmunodeficiency Virus 1 272 Gly Ala Glu Thr Phe Tyr Val Asp Gly Ala 1 510 273 9 PRT Human Immunodeficiency Virus 1 273 Asn Ala Asn Pro Asp CysLys Thr Ile 1 5 274 8 PRT Human Immunodeficiency Virus 1 274 Arg Met TyrSer Pro Thr Ser Ile 1 5 275 10 PRT Human Immunodeficiency Virus 1 275Val Pro Val Trp Lys Glu Ala Thr Thr Thr 1 5 10 276 9 PRT HumanImmunodeficiency Virus 1 276 Ile Ser Pro Arg Thr Leu Asn Ala Trp 1 5 27710 PRT Human Immunodeficiency Virus 1 277 Thr Ser Thr Leu Gln Glu GlnIle Gly Trp 1 5 10 278 11 PRT Human Immunodeficiency Virus 1 278 Lys AlaPhe Ser Pro Glu Val Ile Pro Met Phe 1 5 10 279 9 PRT HumanImmunodeficiency Virus 1 279 Gln Ala Ser Gln Glu Val Lys Asn Trp 1 5 2809 PRT Human Immunodeficiency Virus 1 280 Gln Ala Ser Gln Asp Val Lys AsnTrp 1 5 281 10 PRT Human Immunodeficiency Virus 1 281 His Thr Gln GlyTyr Phe Pro Asp Trp Gln 1 5 10 282 9 PRT Human Immunodeficiency Virus 1282 Tyr Phe Pro Asp Trp Gln Asn Tyr Thr 1 5 283 10 PRT HumanImmunodeficiency Virus 1 283 Thr Ser Thr Leu Gln Glu Gln Ile Gly Trp 1 510 284 10 PRT Human Immunodeficiency Virus 1 284 Arg Leu Arg Pro Gly GlyLys Lys Lys Tyr 1 5 10 285 9 PRT Human Immunodeficiency Virus 1 285 LeuGly Leu Asn Lys Val Arg Met Tyr 1 5 286 12 PRT Human ImmunodeficiencyVirus 1 286 Leu Val Gly Lys Leu Asn Trp Ala Ser Gln Ile Tyr 1 5 10 28710 PRT Human Immunodeficiency Virus 1 287 Ile Leu Lys Glu Pro Val HisGly Val Tyr 1 5 10 288 11 PRT Human Immunodeficiency Virus 1 288 Thr GlnGly Tyr Phe Pro Asp Trp Gln Asn Tyr 1 5 10 289 8 PRT HumanImmunodeficiency Virus 1 289 Ala Val Asp Leu Ser His Phe Leu 1 5 290 8PRT Human Immunodeficiency Virus 1 290 Val Ile Pro Met Phe Ser Ala Leu 15 291 9 PRT Human Immunodeficiency Virus 1 291 Phe Asn Cys Gly Gly GluPhe Phe Tyr 1 5 292 9 PRT Human Immunodeficiency Virus 1 292 Ser Phe AsnCys Gly Gly Glu Phe Phe 1 5 293 10 PRT Human Immunodeficiency Virus 1293 Pro Leu Thr Phe Gly Trp Cys Tyr Lys Leu 1 5 10 294 10 PRT HumanImmunodeficiency Virus 1 294 Val Leu Glu Trp Arg Phe Asp Ser Arg Leu 1 510 295 10 PRT Human Immunodeficiency Virus 1 295 Phe Pro Val Thr Pro GlnVal Pro Leu Arg 1 5 10 296 10 PRT Human Immunodeficiency Virus 1 296 ThrPro Gly Pro Gly Val Arg Tyr Pro Leu 1 5 10 297 9 PRT HumanImmunodeficiency Virus 1 297 Gln Ala Ser Gln Glu Val Lys Asn Trp 1 5 29810 PRT Human Immunodeficiency Virus 1 IIIB 298 Val Pro Leu Asp Glu AspPhe Arg Lys Tyr 1 5 10 299 9 PRT Human Immunodeficiency Virus 1 IIIB 299Asn Pro Asp Ile Val Ile Tyr Gln Tyr 1 5 300 9 PRT Human ImmunodeficiencyVirus 1 IIIB 300 Arg Ala Ile Glu Ala Gln Ala His Leu 1 5 301 8 PRT HumanImmunodeficiency Virus 1 IIIB 301 Thr Ala Phe Thr Ile Pro Ser Ile 1 5302 10 PRT Human Immunodeficiency Virus 1 IIIB 302 Val His Pro Val HisAla Gly Pro Ile Ala 1 5 10 303 10 PRT Human Immunodeficiency Virus 1IIIB 303 Asn Cys Ser Phe Asn Ile Ser Thr Ser Ile 1 5 10 304 9 PRT HumanImmunodeficiency Virus 1 IIIB 304 Cys Thr Asn Val Ser Thr Val Gln Cys 15 305 9 PRT Human Immunodeficiency Virus 1 5F2 305 Ile Gly Pro Gly ArgAla Phe His Thr 1 5 306 9 PRT Human Immunodeficiency Virus 1 5F2 306 AsnPro Asp Ile Val Ile Tyr Gln Tyr 1 5 307 10 PRT Human ImmunodeficiencyVirus 1 5F2 307 Glu Pro Ile Val Gly Ala Glu Thr Phe Tyr 1 5 10 308 9 PRTHuman Immunodeficiency Virus 1 5F2 308 Glu Pro Ile Val Gly Ala Glu ThrPhe 1 5 309 9 PRT Human Immunodeficiency Virus 1 5F2 309 Ser Pro Ala IlePhe Gln Ser Ser Met 1 5 310 10 PRT Human Immunodeficiency Virus 1 5F2310 Val Pro Leu Asp Lys Asp Phe Arg Lys Tyr 1 5 10 311 9 PRT HumanImmunodeficiency Virus 1 5F2 311 Ile Pro Leu Thr Glu Glu Ala Glu Leu 1 5312 11 PRT Human Immunodeficiency Virus 1 5F2 312 Arg Pro Gln Val ProLeu Arg Pro Met Thr Tyr 1 5 10 313 9 PRT Human Immunodeficiency Virus 15F2 313 Phe Pro Val Arg Pro Gln Val Pro Leu 1 5 314 9 PRT HumanImmunodeficiency Virus 1 5F2 314 Asp Pro Asn Pro Gln Glu Val Val Leu 1 5315 9 PRT Human Immunodeficiency Virus 1 5F2 315 Arg Pro Ile Val Ser ThrGln Leu Leu 1 5 316 9 PRT Human Immunodeficiency Virus 1 5F2 316 Ile ProLeu Thr Glu Glu Ala Glu Leu 1 5 317 9 PRT Human Immunodeficiency Virus 15F2 317 Asp Pro Asn Pro Gln Glu Val Val Leu 1 5 318 9 PRT HumanImmunodeficiency Virus 1 5F2 318 Ala Met Gln Met Leu Lys Glu Thr Ile 1 5319 9 PRT Human Immunodeficiency Virus 2 319 Thr Pro Tyr Asp Arg Asn GlnMet Leu 1 5 320 11 PRT Human Immunodeficiency Virus 2 320 Arg Arg TrpIle Gln Leu Gly Leu Gln Lys Val 1 5 10 321 15 PRT Human ImmunodeficiencyVirus 1 5F2 321 Gly Ile Trp Gly Cys Ser Gly Lys Leu Ile Cys Thr Thr AlaVal 1 5 10 15 322 15 PRT Human Immunodeficiency Virus 1 5F2 322 Ala LeuIle Trp Glu Asp Leu Arg Ser Leu Cys Leu Phe Ser Tyr 1 5 10 15 323 9 PRTHuman Papillomavirus 6b 323 Gly Leu His Cys Tyr Glu Gln Leu Val 1 5 3249 PRT Human Papillomavirus 6b 324 Pro Leu Lys Gln His Phe Gln Ile Val 15 325 9 PRT Human Papillomavirus 11 325 Arg Leu Val Thr Leu Lys Asp IleVal 1 5 326 9 PRT Human Papillomavirus 16 326 Thr Leu Gly Ile Val CysPro Ile Cys 1 5 327 9 PRT Human Papillomavirus 16 327 Gly Thr Leu GlyIle Val Cys Pro Ile 1 5 328 9 PRT Human Papillomavirus 16 328 Met LeuAsp Leu Gln Pro Glu Thr Thr 1 5 329 10 PRT Human Papillomavirus 16 329Tyr Met Leu Asp Leu Gln Pro Glu Thr Thr 1 5 10 330 8 PRT HumanPapillomavirus 16 330 Arg Pro Arg Lys Leu Pro Gln Leu 1 5 331 9 PRTHuman Papillomavirus 16 331 Arg Ala His Tyr Asn Ile Val Thr Phe 1 5 3328 PRT Herpes Simplex Virus 332 Ser Ser Ile Glu Phe Ala Arg Leu 1 5 333 9PRT Herpes Simplex Virus 1 333 Gly Ile Gly Ile Gly Val Leu Ala Ala 1 5334 9 PRT Herpes Simplex Virus 1 334 Asp Tyr Ala Thr Leu Gly Val Gly Val1 5 335 11 PRT Herpes Simplex Virus 1 335 Leu Tyr Arg Thr Phe Ala GlyAsn Pro Arg Ala 1 5 10 336 8 PRT Herpes Simplex Virus 1 336 Gln Thr PheAsp Phe Gly Arg Leu 1 5 337 9 PRT Herpes Simplex Virus 2 337 Gly Ala GlyIle Gly Val Ala Val Leu 1 5 338 9 PRT Human T-lymphotropic Virus 1 338Leu Leu Phe Gly Tyr Pro Val Tyr Val 1 5 339 9 PRT Influenza 339 Gly IleLeu Gly Phe Val Phe Thr Leu 1 5 340 10 PRT Influenza 340 Ile Leu Gly PheVal Phe Thr Leu Thr Val 1 5 10 341 9 PRT Influenza 341 Ile Leu Arg GlySer Val Ala His Lys 1 5 342 9 PRT Influenza 342 Lys Thr Gly Gly Pro IleTyr Lys Arg 1 5 343 9 PRT Influenza 343 Glu Leu Arg Ser Arg Tyr Trp AlaIle 1 5 344 8 PRT Influenza 344 Leu Arg Ser Arg Tyr Trp Ala Ile 1 5 3459 PRT Influenza 345 Glu Asp Leu Arg Val Leu Ser Phe Ile 1 5 346 9 PRTInfluenza 346 Gly Glu Ile Ser Pro Leu Pro Ser Leu 1 5 347 9 PRTInfluenza 347 Phe Glu Asp Leu Arg Val Leu Ser Phe 1 5 348 9 PRTInfluenza 348 Gly Glu Ile Ser Pro Leu Pro Ser Leu 1 5 349 9 PRTInfluenza 349 Phe Glu Asp Leu Arg Val Leu Ser Phe 1 5 350 9 PRTInfluenza 350 Val Ser Asp Gly Gly Pro Lys Leu Tyr 1 5 351 9 PRTInfluenza A 351 Cys Thr Glu Leu Lys Leu Ser Asp Tyr 1 5 352 9 PRTInfluenza 352 Ala Ile Met Asp Lys Asn Ile Ile Leu 1 5 353 10 PRTInfluenza A 353 Ile Met Asp Lys Asn Ile Ile Leu Lys Ala 1 5 10 354 9 PRTInfluenza A 354 Ser Arg Tyr Trp Ala Ile Arg Thr Arg 1 5 355 9 PRTInfluenza A 355 Thr Tyr Gln Arg Thr Arg Ala Leu Val 1 5 356 10 PRTInfluenza A 356 Thr Tyr Val Ser Val Ser Thr Ser Thr Leu 1 5 10 357 9 PRTInfluenza A 357 Ile Tyr Ser Thr Val Ala Ser Ser Leu 1 5 358 8 PRTInfluenza A 358 Phe Glu Ala Asn Gly Asn Leu Ile 1 5 359 9 PRT InfluenzaA 359 Ile Glu Gly Gly Trp Thr Gly Met Leu 1 5 360 8 PRT Influenza A 360Ser Asp Tyr Glu Gly Arg Leu Ile 1 5 361 9 PRT Influenza A 361 Glu GluGly Ala Ile Val Gly Glu Ile 1 5 362 9 PRT Influenza A34 362 Ala Ser AsnGlu Asn Met Glu Thr Met 1 5 363 9 PRT Influenza A68 363 Ala Ser Asn GluAsn Met Asp Ala Met 1 5 364 10 PRT Influenza B 364 Lys Leu Gly Glu PheTyr Asn Gln Met Met 1 5 10 365 10 PRT Influenza B 365 Lys Ala Gly GluPhe Tyr Asn Gln Met Met 1 5 10 366 9 PRT Influenza JAP 366 Leu Tyr GlnAsn Val Gly Thr Tyr Val 1 5 367 10 PRT Influenza JAP 367 Thr Tyr Val SerVal Gly Thr Ser Thr Leu 1 5 10 368 9 PRT Influenza JAP 368 Val Tyr GlnIle Leu Ala Thr Tyr Ala 1 5 369 9 PRT Influenza JAP 369 Ile Tyr Ala ThrVal Ala Gly Ser Leu 1 5 370 10 PRT Influenza JAP 370 Thr Tyr Val Ser ValGly Thr Ser Thr Ile 1 5 10 371 8 PRT Influenza JAP 371 Phe Glu Ser ThrGly Asn Leu Ile 1 5 372 9 PRT Mouse Hepatitis Virus Strain JHM 372 AlaPro Thr Ala Gly Ala Phe Phe Phe 1 5 373 9 PRT LymphocyticChoriomeningitis Virus 373 Arg Pro Gln Ala Ser Gly Val Tyr Met 1 5 374 9PRT Lymphocytic Choriomeningitis Virus 374 Phe Gln Pro Gln Asn Gly GlnPhe Ile 1 5 375 11 PRT Lymphocytic Choriomeningitis Virus 375 Ser GlyVal Glu Asn Pro Gly Gly Tyr Cys Leu 1 5 10 376 10 PRT LymphocyticChoriomeningitis Virus 376 Lys Ala Val Tyr Asn Phe Ala Thr Cys Gly 1 510 377 9 PRT Murine Cytomegalovirus 377 Tyr Pro His Phe Met Pro Thr AsnLeu 1 5 378 9 PRT Mouse Hepatitis Virus 378 Cys Leu Ser Trp Asn Gly ProHis Leu 1 5 379 9 PRT Mouse Mammarytumor Virus 379 Ser Phe Ala Val AlaThr Thr Ala Leu 1 5 380 9 PRT Mouse Mammarytumor Virus 380 Ser Tyr GluThr Phe Ile Ser Arg Leu 1 5 381 8 PRT Mouse Mammarytumor Virus 381 AlaAsn Tyr Asp Phe Ile Cys Val 1 5 382 8 PRT Murine Leukemia Virus 382 LysSer Pro Trp Phe Thr Thr Leu 1 5 383 8 PRT Murine Leukemia Virus 383 SerSer Trp Asp Phe Ile Thr Val 1 5 384 9 PRT Murine Leukemia Virus 384 CysCys Leu Cys Leu Thr Val Phe Leu 1 5 385 9 PRT Murine Leukemia Virus 385Ser Pro Ser Tyr Val Tyr His Gln Phe 1 5 386 11 PRT Measles Virus 386 SerArg Arg Tyr Pro Asp Ala Val Tyr Leu His 1 5 10 387 9 PRT Measles Virus387 Arg Arg Tyr Pro Asp Ala Val Tyr Leu 1 5 388 9 PRT Measles Virus 388Tyr Pro Ala Leu Gly Leu His Glu Phe 1 5 389 9 PRT Measles Virus 389 AspPro Val Ile Asp Arg Leu Tyr Leu 1 5 390 9 PRT Measles Virus 390 Ser ProGly Arg Ser Phe Ser Tyr Phe 1 5 391 8 PRT Poliovirus 391 Thr Tyr Lys AspThr Val Gln Leu 1 5 392 10 PRT Poliovirus 392 Phe Tyr Asp Gly Phe SerLys Val Pro Leu 1 5 10 393 9 PRT Pseudorabies virus gp 393 Ile Ala GlyIle Gly Ile Leu Ala Ile 1 5 394 9 PRT Rabiesvirus 394 Val Glu Ala GluIle Ala His Gln Ile 1 5 395 8 PRT Rotavirus 395 Leu Leu Tyr Arg Phe LeuLeu Leu 1 5 396 9 PRT Rotavirus 396 Val Gly Pro Val Phe Pro Pro Gly Met1 5 397 9 PRT Rotavirus 397 Tyr Ser Gly Tyr Ile Phe Arg Asp Leu 1 5 3989 PRT Respiratory Syncytial Virus 398 Ser Tyr Ile Gly Ser Ile Asn AsnIle 1 5 399 12 PRT Simian Immunodeficiency Virus 399 Glu Gly Cys Thr ProTyr Asp Thr Asn Gln Met Leu 1 5 10 400 9 PRT Sendai Virus 400 Phe AlaPro Gly Asn Tyr Pro Ala Leu 1 5 401 10 PRT Sendai Virus 401 Phe Ala ProCys Thr Asn Tyr Pro Ala Leu 1 5 10 402 8 PRT Sendai Virus 40 402 Val ValTyr Asp Phe Leu Lys Cys 1 5 403 10 PRT Sendai Virus 40 403 Ser Ala IleAsn Asn Tyr Ala Gln Lys Leu 1 5 10 404 9 PRT Sendai Virus 40 404 Cys LysGly Val Asn Lys Glu Tyr Leu 1 5 405 9 PRT Sendai Virus 40 405 Gln GlyIle Asn Asn Leu Asp Asn Leu 1 5 406 10 PRT Sendai Virus 40 406 Asn AsnLeu Asp Asn Leu Arg Asp Tyr Leu 1 5 10 407 9 PRT Sendai Virus 40 407 SerGlu Phe Leu Leu Glu Lys Arg Ile 1 5 408 8 PRT Vesicular Stomatitis Virus408 Arg Gly Tyr Val Tyr Gln Gly Leu 1 5 409 9 PRT Homo Sapiens 409 GluAla Asp Pro Thr Gly His Ser Tyr 1 5 410 9 PRT Influenza 410 Val Ser AspGly Gly Pro Asn Leu Tyr 1 5 411 9 PRT Influenza 411 Cys Thr Glu Leu LysLeu Ser Asp Tyr 1 5 412 9 PRT Homo Sapiens 412 Glu Val Asp Pro Ile GlyHis Leu Tyr 1 5 413 10 PRT Homo Sapien (Calreticulin) 413 Met Leu LeuSer Val Pro Leu Leu Leu Gly 1 5 10 414 9 PRT Hepatitis B Virus VARIANT4, 8 Xaa = Any Amino Acid 414 Ser Thr Asx Xaa Gln Ser Gly Xaa Gln 1 5415 9 PRT Homo Sapiens 415 Tyr Met Asp Gly Thr Met Ser Gln Val 1 5 416 9PRT Human Immunodeficiency Virus 1 416 Ile Leu Lys Glu Pro Val His GlyVal 1 5 417 10 PRT Influenza MP 417 Leu Leu Gly Phe Val Phe Thr Leu ThrVal 1 5 10 418 10 PRT Human T-lymphotropic Virus 1 418 Leu Leu Phe GlyTyr Pro Val Tyr Val Val 1 5 10 419 10 PRT Hepatitis B Virus 419 Gly LeuSer Pro Thr Val Trp Leu Ser Val 1 5 10 420 9 PRT Hepatitis B Virus 420Trp Leu Ser Leu Leu Val Pro Phe Val 1 5 421 10 PRT Hepatitis B Virus 421Phe Leu Pro Ser Asp Phe Phe Pro Ser Val 1 5 10 422 8 PRT Epstein-BarrVirus 422 Cys Leu Gly Leu Leu Thr Met Val 1 5 423 11 PRT HumanCytomegalovirus 423 Phe Leu Ala Gly Asn Ser Ala Tyr Glu Tyr Val 1 5 10424 10 PRT Influenza 424 Lys Leu Gly Glu Phe Tyr Asn Gln Met Met 1 5 10425 10 PRT Hepatitis C Virus 1 425 Lys Leu Val Ala Leu Gly Ile Asn AlaVal 1 5 10 426 9 PRT Hepatitis C Virus 426 Asp Leu Met Gly Tyr Ile ProLeu Val 1 5 427 9 PRT Human Papillomavirus 427 Arg Leu Val Thr Leu LysAsp Ile Val 1 5 428 9 PRT Homo Sapien 428 Met Leu Leu Ala Val Leu TyrCys Leu 1 5 429 9 PRT Homo Sapien 429 Ala Ala Gly Ile Gly Ile Leu ThrVal 1 5 430 9 PRT Homo Sapien 430 Tyr Leu Glu Pro Gly Pro Val Thr Ala 15 431 10 PRT Homo Sapien 431 Ile Leu Asp Gly Thr Ala Thr Leu Arg Leu 1 510 432 10 PRT Homo Sapien 432 Leu Leu Asp Gly Thr Ala Thr Leu Arg Leu 15 10 433 9 PRT Homo Sapien 433 Ile Thr Asp Gln Val Pro Phe Ser Val 1 5434 9 PRT Homo Sapien 434 Lys Thr Trp Gly Gln Tyr Trp Gln Val 1 5 435 10PRT Homo Sapien 435 Thr Ile Thr Asp Gln Val Pro Phe Ser Val 1 5 10 43610 PRT Human Immunodeviciency Virus 1 436 Ala Phe His Ile Ile Val AlaArg Glu Leu 1 5 10 437 9 PRT Plasmodium Falciparum 437 Tyr Leu Asn LysIle Gln Asn Ser Leu 1 5 438 10 PRT Plasmodium Falciparum 438 Met Met ArgLys Leu Ala Ile Leu Ser Val 1 5 10 439 10 PRT Influenza 439 Lys Ala GlyGlu Phe Tyr Asn Gln Met Met 1 5 10 440 9 PRT Epstein-Barr Virus (EBNA)440 Asn Ile Ala Glu Gly Leu Arg Ala Leu 1 5 441 9 PRT Epstein-Barr Virus(EBNA) 441 Asn Leu Arg Arg Gly Thr Ala Leu Ala 1 5 442 9 PRTEpstein-Barr Virus (EBNA) 442 Ala Leu Ala Ile Pro Gln Cys Arg Leu 1 5443 9 PRT Epstein-Barr Virus (EBNA) 443 Val Leu Lys Asp Ala Ile Lys AspLeu 1 5 444 9 PRT Epstein-Barr Virus (EBNA) 444 Phe Met Val Phe Leu GlnThr His Ile 1 5 445 9 PRT Epstein-Barr Virus (EBNA) 445 His Leu Ile ValAsp Thr Asp Ser Leu 1 5 446 9 PRT Epstein-Barr Virus (EBNA) 446 Ser LeuGly Asn Pro Ser Leu Ser Val 1 5 447 9 PRT Epstein-Barr Virus (EBNA) 447Pro Leu Ala Ser Ala Met Arg Met Leu 1 5 448 9 PRT Epstein-Barr Virus(EBNA) 448 Arg Met Leu Trp Met Ala Asn Tyr Ile 1 5 449 9 PRTEpstein-Barr Virus (EBNA) 449 Met Leu Trp Met Ala Asn Tyr Ile Val 1 5450 9 PRT Epstein-Barr Virus (EBNA) 450 Ile Leu Pro Gln Gly Pro Gln ThrAla 1 5 451 10 PRT Epstein-Barr Virus (EBNA) 451 Pro Leu Arg Pro Thr AlaPro Thr Thr Ile 1 5 10 452 9 PRT Epstein-Barr Virus (EBNA) 452 Pro LeuPro Pro Ala Thr Leu Thr Val 1 5 453 9 PRT Epstein-Barr Virus (EBNA) 453Arg Met His Leu Pro Val Leu His Val 1 5 454 9 PRT Epstein-Barr Virus(EBNA) 454 Pro Met Pro Leu Pro Pro Ser Gln Leu 1 5 455 9 PRTEpstein-Barr Virus (EBNA) 455 Gln Leu Pro Pro Pro Ala Ala Pro Ala 1 5456 9 PRT Epstein-Barr Virus (EBNA) 456 Ser Met Pro Glu Leu Ser Pro ValLeu 1 5 457 9 PRT Epstein-Barr Virus (EBNA) 457 Asp Leu Asp Glu Ser TrpAsp Tyr Leu 1 5 458 10 PRT Epstein-Barr Virus (EBNA) 458 Pro Leu Pro CysVal Leu Trp Pro Val Val 1 5 10 459 9 PRT Epstein-Barr Virus (EBNA) 459Ser Leu Glu Glu Cys Asp Ser Glu Leu 1 5 460 9 PRT Epstein-Barr Virus(EBNA) 460 Glu Ile Lys Arg Tyr Lys Asn Arg Val 1 5 461 10 PRTEpstein-Barr Virus (EBNA) 461 Gln Leu Leu Gln Phe Ile Tyr Arg Glu Val 15 10 462 9 PRT Epstein-Barr Virus (EBNA) 462 Leu Leu Gln His Tyr Arg GluVal Ala 1 5 463 9 PRT Epstein-Barr Virus (EBNA) 463 Leu Leu Lys Gln MetCys Pro Ser Leu 1 5 464 9 PRT Epstein-Barr Virus (EBNA) 464 Ser Ile IlePro Arg Thr Pro Asp Val 1 5 465 9 PRT Influenza A 465 Ala Ile Met AspLys Asn Ile Ile Leu 1 5 466 10 PRT Influenza A 466 Ile Met Asp Lys AsnIle Ile Leu Lys Ala 1 5 10 467 10 PRT Hepatitis C Virus 467 Leu Leu AlaLeu Leu Ser Cys Leu Thr Val 1 5 10 468 8 PRT Hepatitis C Virus 468 IleLeu His Thr Pro Gly Cys Val 1 5 469 10 PRT Hepatitis C Virus 469 Gln LeuArg Arg His Ile Asp Leu Leu Val 1 5 10 470 9 PRT Hepatitis C Virus 470Asp Leu Cys Gly Ser Val Phe Leu Val 1 5 471 9 PRT Hepatitis C Virus 471Ser Met Val Gly Asn Trp Ala Lys Val 1 5 472 9 PRT Hepatitis C Virus 472His Leu His Gln Asn Ile Val Asp Val 1 5 473 9 PRT Hepatitis C Virus 473Phe Leu Leu Leu Ala Asp Ala Arg Val 1 5 474 13 PRT Hepatitis C Virus 474Gly Leu Arg Asp Leu Ala Val Ala Val Glu Pro Val Val 1 5 10 475 11 PRTHepatitis C Virus 475 Ser Leu Leu Ala Pro Gly Ala Lys Gln Asn Val 1 5 10476 10 PRT Hepatitis C Virus 476 Leu Leu Ala Pro Gly Ala Lys Gln Asn Val1 5 10 477 9 PRT Hepatitis B Virus 477 Phe Leu Leu Ser Leu Gly Ile HisLeu 1 5 478 9 PRT Hepatitis B Virus 478 Ser Leu Tyr Ala Asp Ser Pro SerVal 1 5 479 9 PRT Hepatitis B Virus 479 Gly Leu Ser Arg Tyr Val Ala ArgLeu 1 5 480 9 PRT Homo Sapien 480 Lys Ile Phe Gly Ser Leu Ala Phe Leu 15 481 9 PRT Homo Sapien 481 Glu Leu Val Ser Glu Phe Ser Arg Met 1 5 4829 PRT Human Immunodeficiency Virus 1 482 Lys Leu Thr Pro Leu Cys Val ThrLeu 1 5 483 10 PRT Human Immunodeficiency Virus 1 483 Ser Leu Leu AsnAla Thr Asp Ile Ala Val 1 5 10 484 10 PRT Homo Sapien 484 Val Leu TyrArg Tyr Gly Ser Phe Ser Val 1 5 10 485 9 PRT Homo Sapien 485 Tyr Ile GlyGlu Val Leu Val Ser Val 1 5 486 10 PRT Hepatitis C Virus 486 Leu Leu PheAsn Ile Leu Gly Gly Trp Val 1 5 10 487 10 PRT Hepatitis B Virus 487 LeuLeu Val Pro Phe Val Gln Trp Phe Trp 1 5 10 488 9 PRT Hepatitis B Virus488 Ala Leu Met Pro Leu Tyr Ala Cys Ile 1 5 489 9 PRT Hepatitis C Virus489 Tyr Leu Val Ala Tyr Gln Ala Thr Val 1 5 490 9 PRT Himetobi P Virus(HiPV) 490 Thr Leu Gly Ile Val Cys Pro Ile Cys 1 5 491 10 PRT HepatitisC Virus 491 Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu 1 5 10 492 10 PRTHepatitis B Virus 492 Leu Leu Pro Ile Phe Phe Cys Leu Trp Val 1 5 10 4939 PRT Hepatitis B Virus 493 Tyr Met Asp Asp Val Val Leu Gly Ala 1 5 4949 PRT Human Papillomavirus 494 Gly Thr Leu Gly Ile Val Cys Pro Ile 1 5495 10 PRT Hepatitis C Virus 495 Leu Leu Ala Leu Leu Ser Cys Leu Thr Ile1 5 10 496 9 PRT Human Papillomavirus 496 Met Leu Asp Leu Gln Pro GluThr Thr 1 5 497 9 PRT Hepatitis C Virus 497 Ser Leu Met Ala Phe Thr AlaAla Val 1 5 498 9 PRT Hepatitis C Virus 498 Cys Ile Asn Gly Val Cys TrpThr Val 1 5 499 10 PRT Homo Sapien 499 Val Met Asn Ile Leu Leu Gln TyrVal Val 1 5 10 500 9 PRT Homo Sapien 500 Ile Leu Thr Val Ile Leu Gly ValLeu 1 5 501 9 PRT Homo Sapien 501 Phe Leu Trp Gly Pro Arg Ala Leu Val 15 502 9 PRT Hepatitis C Virus 502 Leu Leu Cys Pro Ala Gly His Ala Val 15 503 9 PRT Hepatitis C Virus 503 Ile Leu Asp Ser Phe Asp Pro Leu Val 15 504 9 PRT Hepatitis B Virus 504 Leu Leu Leu Cys Leu Ile Phe Leu Leu 15 505 10 PRT Hepatitis B Virus 505 Leu Ile Asp Tyr Gln Gly Met Leu ProVal 1 5 10 506 10 PRT Hepatitis B Virus 506 Ser Ile Val Ser Pro Phe IlePro Leu Leu 1 5 10 507 9 PRT Hepatitis B Virus 507 Phe Leu Leu Thr ArgIle Leu Thr Ile 1 5 508 9 PRT Plasmodium Faciparum 508 His Leu Gly AsnVal Lys Tyr Leu Val 1 5 509 9 PRT Plasmodium Faciparum 509 Gly Ile AlaGly Gly Leu Ala Leu Leu 1 5 510 9 PRT Hepatitis C Virus 510 Ile Leu AlaGly Tyr Gly Ala Gly Val 1 5 511 9 PRT Hepatitis C Virus 511 Gly Leu GlnAsp Cys Thr Met Leu Val 1 5 512 10 PRT Hepatitis C Virus 512 Thr Gly AlaPro Val Thr Tyr Ser Thr Tyr 1 5 10 513 10 PRT Human ImmunodeficiencyVirus 1 513 Val Ile Tyr Gln Tyr Met Asp Asp Leu Val 1 5 10 514 10 PRTHomo Sapien 514 Val Leu Pro Asp Val Phe Ile Arg Cys Val 1 5 10 515 9 PRTHomo Sapien 515 Val Leu Pro Asp Val Phe Ile Arg Cys 1 5 516 9 PRT HomoSapien 516 Ala Val Gly Ile Gly Ile Ala Val Val 1 5 517 9 PRT Homo Sapien517 Leu Val Val Leu Gly Leu Leu Ala Val 1 5 518 9 PRT Homo Sapien 518Ala Leu Gly Leu Gly Leu Leu Pro Val 1 5 519 9 PRT Herpes Simplex Virus I519 Gly Ile Gly Ile Gly Val Leu Ala Ala 1 5 520 9 PRT Herpes SimplexVirus 2 520 Gly Ala Gly Ile Gly Val Ala Val Leu 1 5 521 9 PRTPseudorabies Virus 521 Ile Ala Gly Ile Gly Ile Leu Ala Ile 1 5 522 9 PRTAdenovirus 522 Leu Ile Val Ile Gly Ile Leu Ile Leu 1 5 523 9 PRTStreptomyces Lincolnensis 523 Leu Ala Gly Ile Gly Leu Ile Ala Ala 1 5524 9 PRT Yeast (YSA-1) 524 Val Asp Gly Ile Gly Ile Leu Thr Ile 1 5 5259 PRT Bacillus Polymyxa 525 Gly Ala Gly Ile Gly Val Leu Thr Ala 1 5 5269 PRT Escherichia Coli 526 Ala Ala Gly Ile Gly Ile Ile Gln Ile 1 5 527 9PRT Escherichia Coli 527 Gln Ala Gly Ile Gly Ile Leu Leu Ala 1 5 528 11PRT Homo Sapien 528 Lys Ala Arg Asp Pro His Ser Gly His Phe Val 1 5 10529 13 PRT Homo Sapien 529 Lys Ala Cys Asp Pro Ile Ile Ser Gly Ile IlePhe Val 1 5 10 530 11 PRT Homo Sapien 530 Ala Cys Asp Pro Phe Ile SerGly His Phe Val 1 5 10 531 9 PRT Human Immunodeficiency Virus I 531 SerLeu Tyr Asn Thr Val Ala Thr Leu 1 5 532 9 PRT Homo Sapien 532 Glu LeuVal Ser Glu Phe Ser Arg Val 1 5 533 10 PRT Human Immunodeficiency VirusI 533 Arg Gly Pro Gly Arg Ala Phe Val Thr Ile 1 5 10 534 9 PRT HepatitisC Virus 534 His Met Trp Asn Phe Ile Ser Gly Ile 1 5 535 10 PRT HumanCytomegalovirus 535 Asn Leu Val Pro Met Val Ala Thr Val Gln 1 5 10 536 9PRT Human Papillomavirus 536 Gly Leu His Cys Tyr Glu Gln Leu Val 1 5 5379 PRT Human Papillomavirus 537 Pro Leu Lys Gln His Phe Gln Ile Val 1 5538 10 PRT Epstein-Barr Virus (EBNA) 538 Leu Leu Asp Phe Val Arg Phe MetGly Val 1 5 10 539 9 PRT Influenza 539 Ala Ile Met Glu Lys Asn Ile MetLeu 1 5 540 9 PRT Plasmodium Falciparum 540 Tyr Leu Lys Thr Ile Gln AsnSer Leu 1 5 541 9 PRT Plasmodium Falciparum 541 Tyr Leu Asn Lys Ile GlnAsn Ser Leu 1 5 542 10 PRT Human Papillomavirus 542 Tyr Met Leu Asp LeuGln Pro Glu Thr Thr 1 5 10 543 9 PRT Human Papillomavirus 543 Leu LeuMet Gly Thr Leu Gly Ile Val 1 5 544 8 PRT Human Papillomavirus 544 ThrLeu Gly Ile Val Cys Pro Ile 1 5 545 9 PRT Human Immunodeficiency Virus 1545 Thr Leu Thr Ser Cys Asn Thr Ser Val 1 5 546 9 PRT HumanPapillomavirus 546 Lys Leu Pro Gln Leu Cys Thr Glu Leu 1 5 547 9 PRTHuman Papillomavirus 16 547 Thr Ile His Asp Ile Ile Leu Glu Cys 1 5 5489 PRT Human Papillomavirus 16 548 Leu Gly Ile Val Cys Pro Ile Cys Ser 15 549 9 PRT Homo Sapien 549 Val Ile Leu Gly Val Leu Leu Leu Ile 1 5 5509 PRT Homo Sapien 550 Ala Leu Met Asp Lys Ser Leu His Val 1 5 551 9 PRTHomo Sapien 551 Gly Ile Leu Thr Val Ile Leu Gly Val 1 5 552 9 PRTPlasmodium Falciparum 552 Met Ile Asn Ala Tyr Leu Asp Lys Leu 1 5 553 9PRT Homo Sapien 553 Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5 554 10 PRTHepatitis B Virus 554 Phe Leu Pro Ser Asp Phe Phe Pro Ser Val 1 5 10 5559 PRT Epstein-Barr Virus (EBNA) 555 Ser Val Arg Asp Arg Leu Ala Arg Leu1 5 556 9 PRT Homo Sapien 556 Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5557 9 PRT Homo Sapien 557 Phe Ala Tyr Asp Gly Lys Asp Tyr Ile 1 5 558 9PRT Homo Sapien 558 Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5 559 10 PRTHepatitis B Virus 559 Phe Leu Pro Ser Asp Phe Phe Pro Ser Val 1 5 10 5609 PRT Homo Sapien 560 Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5 561 10 PRTHepatitis B Virus 561 Phe Leu Pro Ser Asp Phe Phe Pro Ser Val 1 5 10 5629 PRT Homo Sapien 562 Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5 563 9 PRTHomo Sapien 563 Ala Leu Leu Ala Val Gly Ala Thr Lys 1 5 564 11 PRT HumanImmunodeficiency Virus 1 564 Arg Leu Arg Asp Leu Leu Leu Ile Val Thr Arg1 5 10 565 10 PRT Human Immunodeficiency Virus 1 565 Gln Val Pro Leu ArgPro Met Thr Tyr Lys 1 5 10 566 10 PRT Human Immunodeficiency Virus 1 566Thr Val Tyr Tyr Gly Val Pro Val Trp Lys 1 5 10 567 9 PRT HumanImmunodeficiency Virus 1 567 Arg Leu Arg Pro Gly Gly Lys Lys Lys 1 5 5689 PRT Influenza 568 Ile Leu Arg Gly Ser Val Ala His Lys 1 5 569 9 PRTEpstein-Barr Virus (EBNA) 569 Arg Leu Arg Ala Glu Ala Gly Val Lys 1 5570 11 PRT Human Immunodeficiency Virus 1 570 Arg Leu Arg Asp Leu LeuLeu Ile Val Thr Arg 1 5 10 571 9 PRT Human Immunodeficiency Virus 1 571Val Tyr Tyr Gly Val Pro Val Trp Lys 1 5 572 9 PRT Hepatitis C Virus 572Arg Val Cys Glu Lys Met Ala Leu Tyr 1 5 573 9 PRT Homo Sapien 573 LysIle Phe Ser Glu Val Thr Leu Lys 1 5 574 9 PRT Hepatitis B Virus 574 TyrVal Asn Val Asn Met Gly Leu Lys 1 5 575 9 PRT Epstein-Barr Virus (EBNA)575 Ile Val Thr Asp Phe Ser Val Ile Lys 1 5 576 9 PRT Homo Sapien 576Glu Leu Asn Glu Ala Leu Glu Leu Lys 1 5 577 9 PRT Human ImmunodeficiencyVirus 1 577 Val Pro Leu Arg Pro Met Thr Tyr Lys 1 5 578 9 PRT HumanImmunodeficiency Virus 1 578 Ala Ile Phe Gln Ser Ser Met Thr Lys 1 5 57910 PRT Human Immunodeficiency Virus 1 579 Gln Val Pro Leu Arg Pro MetThr Tyr Lys 1 5 10 580 11 PRT Influenza 580 Thr Ile Asn Tyr Thr Ile PheLys His Cys Val 1 5 10 581 12 PRT Human Immunodeficiency Virus 1 581 AlaAla Val Asp Leu Ser His Phe Leu Lys Glu Lys 1 5 10 582 12 PRT HumanImmunodeficiency Virus 1 582 Ala Cys Gln Gly Val Gly Gly Pro Gly Gly HisLys 1 5 10 583 9 PRT Homo Sapien 583 Ser Tyr Leu Asp Ser Gly Ile His Phe1 5 584 9 PRT Human Immunodeficiency Virus 1 584 Arg Tyr Leu Lys Asp GlnGln Leu Leu 1 5 585 9 PRT Homo Sapien 585 Ala Tyr Gly Leu Asp Phe TyrIle Leu 1 5 586 10 PRT Homo Sapien 586 Ala Phe Leu Pro Trp His Arg LeuPhe Leu 1 5 10 587 9 PRT Homo Sapien 587 Ala Phe Leu Pro Trp His Arg LeuPhe 1 5 588 8 PRT Epstein-Barr Virus (EBNA) 588 Arg Tyr Ser Ile Phe PheAsp Tyr 1 5 589 10 PRT Human Immunodeficiency Virus 1 589 Glu Thr IleAsn Glu Glu Ala Ala Glu Trp 1 5 10 590 11 PRT Hepatitis B Virus 590 SerThr Leu Pro Glu Thr Thr Val Val Arg Arg 1 5 10 591 9 PRT Homo Sapien 591Met Ser Leu Gln Arg Gln Phe Leu Arg 1 5 592 9 PRT Homo Sapien 592 LeuLeu Pro Gly Gly Arg Pro Tyr Arg 1 5 593 9 PRT Human ImmunodeficiencyVirus 593 Ile Val Gly Leu Asn Lys Ile Val Arg 1 5 594 9 PRT Homo Sapien594 Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5 595 9 PRT Homo Sapien 595Glu Val Asp Pro Thr Ser Asn Thr Tyr 1 5 596 9 PRT Homo Sapien 596 GluAla Asp Pro Thr Ser Asn Thr Tyr 1 5 597 9 PRT Homo Sapien 597 Glu AlaAsp Pro Thr Ser Asn Thr Tyr 1 5 598 9 PRT Homo Sapien 598 Glu Val AspPro Ile Gly His Val Tyr 1 5 599 10 PRT Homo Sapien 599 Met Leu Leu AlaVal Leu Tyr Cys Leu Leu 1 5 10 600 9 PRT Homo Sapien 600 Met Leu Leu AlaVal Leu Tyr Cys Leu 1 5 601 10 PRT Homo Sapien 601 Ser Glu Ile Trp ArgAsp Ile Asp Phe Ala 1 5 10 602 9 PRT Homo Sapien 602 Ser Glu Ile Trp ArgAsp Ile Asp Phe 1 5 603 9 PRT Homo Sapien VARIANT 1 Xaa = Any Amino Acid603 Xaa Glu Ile Trp Arg Asp Ile Asp Phe 1 5 604 10 PRT Homo Sapien 604Ser Thr Leu Val Glu Val Thr Leu Gly Val 1 5 10 605 9 PRT Homo Sapien 605Leu Val Glu Val Thr Leu Gly Glu Val 1 5 606 10 PRT Homo Sapien 606 ValIle Phe Ser Lys Ala Ser Glu Tyr Leu 1 5 10 607 9 PRT Homo Sapien 607 IleIle Val Leu Ala Ile Ile Ala Ile 1 5 608 11 PRT Homo Sapien 608 Lys IleTrp Glu Glu Leu Ser Met Leu Glu Tyr 1 5 10 609 9 PRT Homo Sapien 609 LeuIle Glu Thr Ser Tyr Val Lys Val 1 5 610 9 PRT Homo Sapien 610 Phe LeuTrp Gly Pro Arg Ala Leu Val 1 5 611 10 PRT Homo Sapien 611 Thr Leu ValGlu Val Thr Leu Gly Glu Val 1 5 10 612 10 PRT Homo Sapien 612 Ala LeuVal Glu Thr Ser Tyr Val Lys Val 1 5 10 613 9 PRT Homo Sapien 613 Lys IleTrp Glu Glu Leu Ser Val Leu 1 5 614 9 PRT Homo Sapien 614 Glu Val AspPro Ile Gly His Leu Tyr 1 5 615 9 PRT Homo Sapien VARIANT 2, 4, 5, 6, 7,8 Xaa = Any Amino Acid 615 Glu Xaa Asp Xaa Xaa Xaa Xaa Xaa Tyr 1 5 616 9PRT Homo Sapien 616 Glu Ala Asp Pro Thr Gly His Ser Tyr 1 5 617 9 PRTHomo Sapien VARIANT 4, 5, 6, 7, 8 Xaa = Any Amino Acid 617 Glu Xaa AspXaa Xaa Xaa Xaa Xaa Tyr 1 5 618 9 PRT Homo Sapien VARIANT 5, 6, 7, 8 Xaa= Any Amino Acid 618 Glu Xaa Asp Pro Xaa Xaa Xaa Xaa Tyr 1 5 619 9 PRTHomo Sapien VARIANT 6, 7, 8 Xaa = Any Amino Acid 619 Glu Xaa Asp Pro XaaXaa Xaa Xaa Tyr 1 5 620 9 PRT Homo Sapien VARIANT 7, 8 Xaa = Any AminoAcid 620 Glu Xaa Asp Pro Xaa Xaa Xaa Xaa Tyr 1 5 621 9 PRT Homo SapienVARIANT 8 Xaa = Any Amino Acid 621 Glu Xaa Asp Pro Xaa Xaa Xaa Xaa Tyr 15 622 9 PRT Homo Sapien VARIANT 2 Xaa = A or V 622 Glu Xaa Asp Pro XaaXaa Xaa Xaa Tyr 1 5 623 16 PRT Homo Sapien 623 Glu Leu His Ser Ala TyrGly Glu Pro Arg Lys Leu Leu Thr Gln Asp 1 5 10 15 624 12 PRT Homo Sapien624 Glu His Ser Ala Tyr Gly Glu Pro Arg Lys Leu Leu 1 5 10 625 9 PRTHomo Sapien 625 Ser Ala Tyr Gly Glu Pro Arg Lys Leu 1 5 626 9 PRT HomoSapien 626 Glu Ala Asp Pro Thr Gly His Ser Tyr 1 5 627 22 PRT HomoSapien 627 Met Ala Ala Arg Ala Val Phe Leu Ala Leu Ser Ala Gln Leu LeuGln 1 5 10 15 Ala Arg Leu Met Lys Glu 20 628 16 PRT Homo Sapien 628 MetAla Ala Arg Ala Val Phe Leu Ala Leu Ser Ala Gln Leu Leu Gln 1 5 10 15629 9 PRT Homo Sapien 629 Ala Ala Arg Ala Val Phe Leu Ala Leu 1 5 630 8PRT Homo Sapien 630 Tyr Arg Pro Arg Pro Arg Arg Tyr 1 5 631 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 631 Ala LeuPhe Ala Ala Ala Ala Ala Val 1 5 632 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 632 Gly Ile Phe Gly Gly Val Gly Gly Val 15 633 8 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide633 Gly Leu Asp Lys Gly Gly Gly Val 1 5 634 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 634 Gly Leu Phe Gly Gly Phe GlyGly Val 1 5 635 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 635 Gly Leu Phe Gly Gly Gly Ala Gly Val 1 5 636 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 636 Gly LeuPhe Gly Gly Gly Glu Gly Val 1 5 637 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 637 Gly Leu Phe Gly Gly Gly Phe Gly Val 15 638 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide638 Gly Leu Phe Gly Gly Gly Gly Gly Leu 1 5 639 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 639 Gly Leu Phe GlyGly Gly Gly Gly Val 1 5 640 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 640 Gly Leu Phe Gly Gly Gly Val Gly Val 1 5 6419 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 641Gly Leu Phe Gly Gly Val Gly Gly Val 1 5 642 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 642 Gly Leu Phe Gly Gly Val GlyLys Val 1 5 643 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 643 Gly Leu Phe Lys Gly Val Gly Gly Val 1 5 644 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 644 Gly LeuGly Gly Gly Gly Phe Gly Val 1 5 645 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 645 Gly Leu Leu Gly Gly Gly Val Gly Val 15 646 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide646 Gly Leu Tyr Gly Gly Gly Gly Gly Val 1 5 647 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 647 Gly Met Phe GlyGly Gly Gly Gly Val 1 5 648 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 648 Gly Met Phe Gly Gly Val Gly Gly Val 1 5 6499 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 649Gly Gln Phe Gly Gly Val Gly Gly Val 1 5 650 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 650 Gly Val Phe Gly Gly Val GlyGly Val 1 5 651 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 651 Lys Leu Phe Gly Gly Gly Gly Gly Val 1 5 652 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 652 Lys LeuPhe Gly Gly Val Gly Gly Val 1 5 653 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 653 Ala Ile Leu Gly Phe Val Phe Thr Leu 15 654 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide654 Gly Ala Ile Gly Phe Val Phe Thr Leu 1 5 655 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 655 Gly Ala Leu GlyPhe Val Phe Thr Leu 1 5 656 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 656 Gly Glu Leu Gly Phe Val Phe Thr Leu 1 5 6579 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 657Gly Ile Ala Gly Phe Val Phe Thr Leu 1 5 658 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 658 Gly Ile Glu Gly Phe Val PheThr Leu 1 5 659 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 659 Gly Ile Leu Ala Phe Val Phe Thr Leu 1 5 660 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 660 Gly IleLeu Gly Ala Val Phe Thr Leu 1 5 661 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 661 Gly Ile Leu Gly Glu Val Phe Thr Leu 15 662 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide662 Gly Ile Leu Phe Gly Ala Phe Thr Leu 1 5 663 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 663 Gly Ile Leu GlyPhe Glu Phe Thr Leu 1 5 664 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 664 Gly Ile Leu Gly Phe Lys Phe Thr Leu 1 5 6659 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 665Gly Ile Leu Gly Phe Val Ala Thr Leu 1 5 666 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 666 Gly Ile Leu Gly Phe Val GluThr Leu 1 5 667 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 667 Gly Ile Leu Gly Phe Val Phe Ala Leu 1 5 668 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 668 Gly IleLeu Gly Phe Val Phe Glu Leu 1 5 669 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 669 Gly Ile Leu Gly Phe Val Phe Lys Leu 15 670 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide670 Gly Ile Leu Gly Phe Val Phe Thr Ala 1 5 671 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 671 Gly Ile Leu GlyPhe Val Phe Thr Leu 1 5 672 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 672 Gly Ile Leu Gly Phe Val Phe Val Leu 1 5 6739 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 673Gly Ile Leu Gly Phe Val Lys Thr Leu 1 5 674 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 674 Gly Ile Leu Gly Lys Val PheThr Leu 1 5 675 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 675 Gly Ile Leu Lys Phe Val Phe Thr Leu 1 5 676 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 676 Gly IleLeu Pro Phe Val Phe Thr Leu 1 5 677 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 677 Gly Ile Val Gly Phe Val Phe Thr Leu 15 678 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide678 Gly Lys Leu Gly Phe Val Phe Thr Leu 1 5 679 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 679 Gly Leu Leu GlyPhe Val Phe Thr Leu 1 5 680 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 680 Gly Gln Leu Gly Phe Val Phe Thr Leu 1 5 6819 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 681Lys Ala Leu Gly Phe Val Phe Thr Leu 1 5 682 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 682 Lys Ile Leu Gly Phe Val PheThr Leu 1 5 683 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 683 Lys Ile Leu Gly Lys Val Phe Thr Leu 1 5 684 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 684 Ala IleLeu Leu Gly Val Phe Met Leu 1 5 685 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 685 Ala Ile Tyr Lys Arg Trp Ile Ile Leu 15 686 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide686 Ala Leu Phe Phe Phe Asp Ile Asp Leu 1 5 687 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 687 Ala Thr Val GluLeu Leu Ser Glu Leu 1 5 688 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 688 Cys Leu Phe Gly Tyr Pro Val Tyr Val 1 5 6899 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 689Phe Ile Phe Pro Asn Tyr Thr Ile Val 1 5 690 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 690 Ile Ile Ser Leu Trp Asp SerGln Leu 1 5 691 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 691 Ile Leu Ala Ser Leu Phe Ala Ala Val 1 5 692 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 692 Ile LeuGlu Ser Leu Phe Ala Ala Val 1 5 693 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 693 Lys Leu Gly Glu Phe Phe Asn Gln Met 15 694 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide694 Lys Leu Gly Glu Phe Tyr Asn Gln Met 1 5 695 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 695 Leu Leu Phe GlyTyr Pro Val Tyr Val 1 5 696 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 696 Leu Leu Trp Lys Gly Glu Gly Ala Val 1 5 6979 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 697Leu Met Phe Gly Tyr Pro Val Tyr Val 1 5 698 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 698 Leu Asn Phe Gly Tyr Pro ValTyr Val 1 5 699 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 699 Leu Gln Phe Gly Tyr Pro Val Tyr Val 1 5 700 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 700 Asn IleVal Ala His Thr Phe Lys Val 1 5 701 8 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 701 Asn Leu Pro Met Val Ala Thr Val 1 5702 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide702 Gln Met Leu Leu Ala Ile Ala Arg Leu 1 5 703 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 703 Gln Met Trp GlnAla Arg Leu Thr Val 1 5 704 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 704 Arg Leu Leu Gln Thr Gly Ile His Val 1 5 7059 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 705Arg Leu Val Asn Gly Ser Leu Ala Leu 1 5 706 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 706 Ser Leu Tyr Asn Thr Val AlaThr Leu 1 5 707 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 707 Thr Leu Asn Ala Trp Val Lys Val Val 1 5 708 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 708 Trp LeuTyr Arg Glu Thr Cys Asn Leu 1 5 709 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 709 Tyr Leu Phe Lys Arg Met Ile Asp Leu 15 710 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide710 Gly Ala Phe Gly Gly Val Gly Gly Val 1 5 711 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 711 Gly Ala Phe GlyGly Val Gly Gly Tyr 1 5 712 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 712 Gly Glu Phe Gly Gly Val Gly Gly Val 1 5 7139 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 713Gly Gly Phe Gly Gly Val Gly Gly Val 1 5 714 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 714 Gly Ile Phe Gly Gly Gly GlyGly Val 1 5 715 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 715 Gly Ile Gly Gly Phe Gly Gly Gly Leu 1 5 716 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 716 Gly IleGly Gly Gly Gly Gly Gly Leu 1 5 717 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 717 Gly Leu Asp Gly Gly Gly Gly Gly Val 15 718 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide718 Gly Leu Asp Gly Lys Gly Gly Gly Val 1 5 719 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 719 Gly Leu Asp LysLys Gly Gly Gly Val 1 5 720 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 720 Gly Leu Phe Gly Gly Gly Phe Gly Phe 1 5 7219 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 721Gly Leu Phe Gly Gly Gly Phe Gly Gly 1 5 722 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 722 Gly Leu Phe Gly Gly Gly PheGly Asn 1 5 723 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 723 Gly Leu Phe Gly Gly Gly Phe Gly Ser 1 5 724 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 724 Gly LeuPhe Gly Gly Gly Gly Gly Ile 1 5 725 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 725 Gly Leu Phe Gly Gly Gly Gly Gly Met 15 726 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide726 Gly Leu Phe Gly Gly Gly Gly Gly Thr 1 5 727 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 727 Gly Leu Phe GlyGly Gly Gly Gly Tyr 1 5 728 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 728 Gly Leu Gly Phe Gly Gly Gly Gly Val 1 5 7299 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 729Gly Leu Gly Gly Phe Gly Gly Gly Val 1 5 730 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 730 Gly Leu Gly Gly Gly Phe GlyGly Val 1 5 731 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 731 Gly Leu Gly Gly Gly Gly Gly Phe Val 1 5 732 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 732 Gly LeuGly Gly Gly Gly Gly Gly Tyr 1 5 733 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 733 Gly Leu Gly Gly Gly Val Gly Gly Val 15 734 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide734 Gly Leu Leu Gly Gly Gly Gly Gly Val 1 5 735 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 735 Gly Leu Pro GlyGly Gly Gly Gly Val 1 5 736 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 736 Gly Asn Phe Gly Gly Val Gly Gly Val 1 5 7379 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 737Gly Ser Phe Gly Gly Val Gly Gly Val 1 5 738 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 738 Gly Thr Phe Gly Gly Val GlyGly Val 1 5 739 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 739 Ala Gly Asn Ser Ala Tyr Glu Tyr Val 1 5 740 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 740 Gly LeuPhe Pro Gly Gln Phe Ala Tyr 1 5 741 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 741 His Ile Leu Leu Gly Val Phe Met Leu 15 742 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide742 Ile Leu Glu Ser Leu Phe Arg Ala Val 1 5 743 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 743 Lys Lys Lys TyrLys Leu Lys His Ile 1 5 744 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 744 Met Leu Ala Ser Ile Asp Leu Lys Tyr 1 5 7459 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 745Met Leu Glu Arg Glu Leu Val Arg Lys 1 5 746 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 746 Lys Leu Phe Gly Phe Val PheThr Val 1 5 747 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 747 Ile Leu Asp Lys Lys Val Glu Lys Val 1 5 748 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 748 Ile LeuLys Glu Pro Val His Gly Val 1 5 749 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 749 Ala Leu Phe Ala Ala Ala Ala Ala Tyr 15 750 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide750 Gly Ile Gly Phe Gly Gly Gly Gly Leu 1 5 751 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 751 Gly Lys Phe GlyGly Val Gly Gly Val 1 5 752 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 752 Gly Leu Phe Gly Gly Gly Gly Gly Lys 1 5 7539 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide 753Glu Ile Leu Gly Phe Val Phe Thr Leu 1 5 754 9 PRT Artificial SequenceSynthetic HLA-A2 binding nonamer peptide 754 Gly Ile Lys Gly Phe Val PheThr Leu 1 5 755 9 PRT Artificial Sequence Synthetic HLA-A2 bindingnonamer peptide 755 Gly Gln Leu Gly Phe Val Phe Thr Lys 1 5 756 9 PRTArtificial Sequence Synthetic HLA-A2 binding nonamer peptide 756 Ile LeuGly Phe Val Phe Thr Leu Thr 1 5 757 9 PRT Artificial Sequence SyntheticHLA-A2 binding nonamer peptide 757 Lys Ile Leu Gly Phe Val Phe Thr Lys 15 758 9 PRT Artificial Sequence Synthetic HLA-A2 binding nonamer peptide758 Lys Lys Leu Gly Phe Val Phe Thr Leu 1 5 759 9 PRT ArtificialSequence Synthetic HLA-A2 binding nonamer peptide 759 Lys Leu Phe GluLys Val Tyr Asn Tyr 1 5 760 9 PRT Artificial Sequence Synthetic HLA-A2binding nonamer peptide 760 Leu Arg Phe Gly Tyr Pro Val Tyr Val 1 5 7619 PRT Homo Sapien 761 Ile Arg Arg Gly Val Met Leu Ala Val 1 5 762 9 PRTHomo Sapien 762 Lys Arg Ile Gln Glu Ile Ile Glu Gln 1 5 763 9 PRT HomoSapien 763 Lys Arg Thr Leu Lys Ile Pro Ala Met 1 5 764 9 PRT YerseniaPestis 764 Gly Arg Asn Val Val Leu Asp Lys Ser 1 5 765 9 PRT YerseniaPestis 765 Lys Arg Gly Ile Asp Lys Ala Val Ile 1 5 766 9 PRT YerseniaPestis 766 Ile Arg Ala Ala Ser Ala Ile Thr Ala 1 5 767 9 PRT YerseniaPestis 767 Arg Arg Lys Ala Met Phe Glu Asp Ile 1 5 768 8 PRT PlasmodiumFalciparum 768 Lys Pro Lys Asp Glu Leu Asp Tyr 1 5 769 9 PRT Influenza769 Leu Glu Leu Arg Ser Arg Tyr Trp Ala 1 5 770 10 PRT Homo Sapien 770Gly Pro Pro His Ser Asn Asn Phe Gly Tyr 1 5 10 771 8 PRT Rotavirus 771Ile Ile Tyr Arg Phe Leu Leu Ile 1 5 772 9 PRT Homo Sapien 772 Gln LeuSer Pro Tyr Pro Phe Asp Leu 1 5 773 8 PRT Homo Sapien 773 Val Tyr AspPhe Phe Val Trp Leu 1 5 774 8 PRT Homo Sapien 774 Ser Asn Phe Val PheAla Gly Ile 1 5 775 8 PRT Rotavirus 775 Ser Val Val Glu Phe Ser Ser Leu1 5 776 8 PRT Artificial Sequence Epitope mimic of natural tumor Ag 776Ala His Tyr Leu Phe Arg Asn Leu 1 5 777 8 PRT Artificial SequenceEpitope mimic of natural tumor Ag 777 Thr His Tyr Leu Phe Arg Asn Leu 15 778 8 PRT Artificial Sequence Epitope Mimic of H-3 miHAg 778 Leu IleVal Ile Tyr Asn Thr Leu 1 5 779 8 PRT Artificial Sequence Epitope Mimicof H-3 miHAg 779 Leu Ile Tyr Glu Phe Asn Thr Leu 1 5 780 8 PRTArtificial Sequence Epitope Mimic of H-3 miHAg 780 Ile Pro Tyr Ile TyrAsn Thr Leu 1 5 781 8 PRT Artificial Sequence Epitope Mimic of H-3 miHAg781 Ile Ile Tyr Ile Tyr His Arg Leu 1 5 782 8 PRT Artificial SequenceEpitope Mimic of H-3 miHAg 782 Leu Ile Tyr Ile Phe Asn Thr Leu 1 5 783 8PRT Hepatitis B Virus 783 Met Gly Leu Lys Phe Arg Gln Leu 1 5 784 9 PRTHomo Sapien 784 Ile Met Ile Lys Phe Arg Asn Arg Leu 1 5 785 9 PRT MusMusculus 785 Trp Met His His Asn Met Asp Leu Ile 1 5 786 9 PRT MusMusculus 786 Lys Tyr Met Cys Asn Ser Ser Cys Met 1 5 787 9 PRT MusMusculus 787 Gly Arg Pro Lys Asn Gly Cys Ile Val 1 5 788 9 PRTArtificial Sequence Epitope mimic of natural tumor Ag 788 Ala Gln HisPro Asn Ala Glu Leu Leu 1 5 789 9 PRT Murine Leukemia Virus 789 Cys CysLeu Cys Leu Thr Val Phe Leu 1 5 790 8 PRT Plasmodium Falciparum 790 TyrGlu Asn Asp Ile Glu Lys Lys 1 5 791 9 PRT Plasmodium Falciparum 791 AspGlu Leu Asp Tyr Glu Asn Asp Ile 1 5 792 9 PRT Human ImmunodeficiencyVirus 792 Thr Glu Met Glu Lys Glu Gly Lys Ile 1 5 793 9 PRT Rabies 793Val Glu Ala Glu Ile Ala His Gln Ile 1 5 794 9 PRT Influenza A 794 GluGlu Gly Ala Ile Val Gly Glu Ile 1 5 795 8 PRT Mus Musculus 795 Thr GluAsn Ser Gly Lys Asp Ile 1 5 796 9 PRT Artificial Sequence MHC Class ILeader 796 Ala Met Ala Pro Arg Thr Leu Leu Leu 1 5 797 11 PRT HomoSapien 797 Phe Phe Ile Asn Ile Leu Thr Leu Leu Val Pro 1 5 10 798 11 PRTHomo Sapien 798 Phe Phe Ile Asn Ile Leu Thr Leu Leu Val Pro 1 5 10 79916 PRT Homo Sapien 799 Phe Phe Ile Asn Ile Leu Thr Leu Leu Val Pro IleLeu Ile Ala Met 1 5 10 15 800 16 PRT Homo Sapien 800 Phe Phe Ile Asn AlaLeu Thr Leu Leu Val Pro Ile Leu Ile Ala Met 1 5 10 15 801 5 PRT HomoSapien 801 Phe Ile Asn Arg Trp 1 5 802 5 PRT Listeria Monocytogenes 802Ile Gly Trp Ile Ile 1 5 803 12 PRT Simian Immunodeficiency Virus 803 GluGly Cys Thr Pro Tyr Asp Ile Asn Gln Met Leu 1 5 10 804 9 PRT Homo Sapien804 Ala Leu Ser Arg Lys Val Ala Glu Leu 1 5 805 9 PRT Homo Sapien 805Ile Met Pro Lys Ala Gly Leu Leu Ile 1 5 806 9 PRT Homo Sapien 806 LysIle Trp Glu Glu Leu Ser Val Leu 1 5 807 10 PRT Homo Sapien 807 Ala LeuVal Glu Thr Ser Tyr Val Lys Val 1 5 10 808 10 PRT Homo Sapien 808 ThrLeu Val Glu Val Thr Leu Gly Glu Val 1 5 10 809 9 PRT Homo Sapien 809 AlaLeu Ser Arg Lys Val Ala Glu Leu 1 5 810 9 PRT Homo Sapien 810 Ile MetPro Lys Ala Gly Leu Leu Ile 1 5 811 9 PRT Homo Sapien 811 Lys Ile TrpGlu Glu Leu Ser Val Leu 1 5 812 10 PRT Homo Sapien 812 Ala Leu Val GluThr Ser Tyr Val Lys Val 1 5 10 813 12 PRT Homo Sapien 813 Lys Gly IleLeu Gly Phe Val Phe Thr Leu Thr Val 1 5 10 814 9 PRT Homo Sapien 814 GlyIle Ile Gly Phe Val Phe Thr Ile 1 5 815 9 PRT Homo Sapien 815 Gly IleIle Gly Phe Val Phe Thr Leu 1 5 816 9 PRT Homo Sapien 816 Gly Ile LeuGly Phe Val Phe Thr Leu 1 5 817 9 PRT Homo Sapien 817 Gly Leu Leu GlyPhe Val Phe Thr Leu 1 5 818 9 PRT Homo Sapien VARIANT 1, 2, 5, 6, 9 Xaa= Any Amino Acid 818 Xaa Xaa Thr Val Xaa Xaa Gly Val Xaa 1 5 819 9 PRTHomo Sapien 819 Ile Leu Thr Val Ile Leu Gly Val Leu 1 5 820 9 PRT HomoSapien 820 Tyr Leu Glu Pro Gly Pro Val Thr Ala 1 5 821 10 PRT HomoSapien 821 Gln Val Pro Leu Arg Pro Met Thr Tyr Lys 1 5 10 822 11 PRTHomo Sapien 822 Asp Gly Leu Ala Pro Pro Gln His Leu Ile Arg 1 5 10 823 9PRT Homo Sapien 823 Leu Leu Gly Arg Asn Ser Phe Glu Val 1 5 824 16 PRTHomo Sapien 824 Glu His Ser Ala Tyr Gly Glu Pro Arg Lys Leu Leu Thr GlnAsp Leu 1 5 10 15 825 12 PRT Homo Sapien 825 Glu His Ser Ala Tyr Gly GluPro Arg Lys Leu Leu 1 5 10 826 9 PRT Homo Sapien 826 Ser Ala Tyr Gly GluPro Arg Lys Leu 1 5 827 8 PRT Homo Sapien 827 Tyr Arg Pro Arg Pro ArgArg Tyr 1 5 828 9 PRT Homo Sapien 828 Thr Tyr Arg Pro Arg Pro Arg ArgTyr 1 5 829 9 PRT Homo Sapien 829 Tyr Arg Pro Arg Pro Arg Arg Tyr Val 15 830 10 PRT Homo Sapien 830 Thr Tyr Arg Pro Arg Pro Arg Arg Tyr Val 1 510 831 9 PRT Homo Sapien 831 Arg Pro Arg Pro Arg Arg Tyr Val Glu 1 5 83215 PRT Homo Sapien 832 Met Ser Trp Arg Gly Arg Ser Thr Tyr Arg Pro ArgPro Arg Arg 1 5 10 15 833 16 PRT Homo Sapien 833 Thr Tyr Arg Pro Arg ProArg Arg Tyr Val Glu Pro Pro Glu Met Ile 1 5 10 15 834 3 PRT Homo Sapien834 Glu Asp Tyr 1 835 9 PRT Homo Sapien 835 Glu Val Val Pro Ile Ser HisLeu Tyr 1 5 836 9 PRT Homo Sapien 836 Glu Val Val Arg Ile Gly His LeuTyr 1 5 837 9 PRT Homo Sapien 837 Glu Val Asp Pro Ile Gly His Leu Tyr 15 838 9 PRT Homo Sapien 838 Glu Val Asp Pro Ala Ser Asn Thr Tyr 1 5 8399 PRT Homo Sapien 839 Glu Val Asp Pro Thr Ser Asn Thr Tyr 1 5 840 9 PRTHomo Sapien 840 Glu Ala Asp Pro Thr Ser Asn Thr Tyr 1 5 841 9 PRT HomoSapien 841 Glu Val Asp Pro Ile Gly His Val Tyr 1 5 842 27 DNA HomoSapien 842 gaagtggtcc ccatcagcca cttgtac 27 843 27 DNA Homo Sapien 843gaagtggtcc gcatcggcca cttgtac 27 844 27 DNA Homo Sapien 844 gaagtggaccccatcggcca cttgtac 27 845 27 DNA Homo Sapien 845 gaagtggacc ccgccagcaacacctac 27 846 27 DNA Homo Sapien 846 gaagtggacc ccaccagcaa cacctac 27847 27 DNA Homo Sapien 847 gaagcggacc ccaccagcaa cacctac 27 848 27 DNAHomo Sapien 848 gaagcggacc ccaccagcaa cacctac 27 849 27 DNA Homo Sapien849 gaagtggacc ccatcggcca cgtgtac 27 850 8 PRT Homo Sapien 850 Glu AlaAsp Pro Thr Gly His Ser 1 5 851 8 PRT Homo Sapien 851 Ala Asp Pro TrpGly His Ser Tyr 1 5 852 11 PRT Homo Sapien 852 Ser Thr Leu Val Glu ValThr Leu Gly Glu Val 1 5 10 853 9 PRT Homo Sapien 853 Leu Val Glu Val ThrLeu Gly Glu Val 1 5 854 9 PRT Homo Sapien 854 Lys Met Val Glu Leu ValHis Phe Leu 1 5 855 10 PRT Homo Sapien 855 Val Ile Phe Ser Lys Ala SerGlu Tyr Leu 1 5 10 856 10 PRT Homo Sapien 856 Tyr Leu Gln Leu Val PheGly Ile Glu Val 1 5 10 857 9 PRT Homo Sapien 857 Gln Leu Val Phe Gly IleGlu Val Val 1 5 858 11 PRT Homo Sapien 858 Gln Leu Val Phe Gly Ile GluVal Val Glu Val 1 5 10 859 9 PRT Homo Sapien 859 Ile Ile Val Leu Ala IleIle Ala Ile 1 5 860 11 PRT Homo Sapien 860 Lys Ile Trp Glu Glu Leu SerMet Leu Glu Val 1 5 10 861 10 PRT Homo Sapien 861 Ala Leu Ile Glu ThrSer Tyr Val Lys Val 1 5 10 862 9 PRT Homo Sapien 862 Leu Ile Glu Thr SerTyr Val Lys Val 1 5 863 11 PRT Homo Sapien 863 Gly Leu Glu Ala Arg GlyGlu Ala Leu Gly Leu 1 5 10 864 9 PRT Homo Sapien 864 Gly Leu Glu Ala ArgGly Glu Ala Leu 1 5 865 9 PRT Homo Sapien 865 Ala Leu Gly Leu Val GlyAla Gln Ala 1 5 866 9 PRT Homo Sapien 866 Gly Leu Val Gly Ala Gln AlaPro Ala 1 5 867 9 PRT Homo Sapien 867 Asp Leu Glu Ser Glu Phe Gln AlaAla 1 5 868 10 PRT Homo Sapien 868 Asp Leu Glu Ser Glu Phe Gln Ala AlaIle 1 5 10 869 10 PRT Homo Sapien 869 Ala Ile Ser Arg Lys Met Val GluLeu Val 1 5 10 870 9 PRT Homo Sapien 870 Ala Ile Ser Arg Lys Met Val GluLeu 1 5 871 10 PRT Homo Sapien 871 Lys Met Val Glu Leu Val His Phe LeuLeu 1 5 10 872 11 PRT Homo Sapien 872 Lys Met Val Glu Leu Val His PheLeu Leu Leu 1 5 10 873 11 PRT Homo Sapien 873 Leu Leu Leu Lys Tyr ArgAla Arg Glu Pro Val 1 5 10 874 10 PRT Homo Sapien 874 Leu Leu Lys TyrArg Ala Arg Glu Pro Val 1 5 10 875 11 PRT Homo Sapien 875 Val Leu ArgAsn Cys Gln Asp Phe Phe Pro Val 1 5 10 876 11 PRT Homo Sapien 876 TyrLeu Gln Leu Val Phe Gly Ile Glu Val Val 1 5 10 877 10 PRT Homo Sapien877 Gly Ile Glu Val Val Glu Val Val Pro Ile 1 5 10 878 9 PRT Homo Sapien878 Pro Ile Ser His Leu Tyr Ile Leu Val 1 5 879 9 PRT Homo Sapien 879His Leu Tyr Ile Leu Val Thr Cys Leu 1 5 880 11 PRT Homo Sapien 880 HisLeu Tyr Ile Leu Val Thr Cys Leu Gly Leu 1 5 10 881 9 PRT Homo Sapien 881Tyr Ile Leu Val Thr Cys Leu Gly Leu 1 5 882 9 PRT Homo Sapien 882 CysLeu Gly Leu Ser Tyr Asp Gly Leu 1 5 883 10 PRT Homo Sapien 883 Cys LeuGly Leu Ser Tyr Asp Gly Leu Leu 1 5 10 884 9 PRT Homo Sapien 884 Val MetPro Lys Thr Gly Leu Leu Ile 1 5 885 10 PRT Homo Sapien 885 Val Met ProLys Thr Gly Leu Leu Ile Ile 1 5 10 886 11 PRT Homo Sapien 886 Val MetPro Lys Thr Gly Leu Leu Ile Ile Val 1 5 10 887 9 PRT Homo Sapien 887 GlyLeu Leu Ile Ile Val Leu Ala Ile 1 5 888 10 PRT Homo Sapien 888 Gly LeuLeu Ile Ile Val Leu Ala Ile Ile 1 5 10 889 11 PRT Homo Sapien 889 GlyLeu Leu Ile Ile Val Leu Ala Ile Ile Ala 1 5 10 890 9 PRT Homo Sapien 890Leu Leu Ile Ile Val Leu Ala Ile Ile 1 5 891 10 PRT Homo Sapien 891 LeuLeu Ile Ile Val Leu Ala Ile Ile Ala 1 5 10 892 11 PRT Homo Sapien 892Leu Leu Ile Ile Val Leu Ala Ile Ile Ala Ile 1 5 10 893 9 PRT Homo Sapien893 Leu Ile Ile Val Leu Ala Ile Ile Ala 1 5 894 10 PRT Homo Sapien 894Leu Ile Ile Val Leu Ala Ile Ile Ala Ile 1 5 10 895 9 PRT Homo Sapien 895Ile Ile Ala Ile Glu Gly Asp Cys Ala 1 5 896 9 PRT Homo Sapien 896 LysIle Trp Glu Glu Leu Ser Met Leu 1 5 897 11 PRT Homo Sapien 897 Leu MetGln Asp Leu Val Gln Glu Asn Tyr Leu 1 5 10 898 9 PRT Homo Sapien 898 PheLeu Trp Gly Pro Arg Ala Leu Ile 1 5 899 9 PRT Homo Sapien 899 Leu IleGlu Thr Ser Tyr Val Lys Val 1 5 900 11 PRT Homo Sapien 900 Ala Leu IleGlu Thr Ser Tyr Val Lys Val Leu 1 5 10 901 10 PRT Homo Sapien 901 ThrLeu Lys Ile Gly Gly Glu Pro His Ile 1 5 10 902 11 PRT Homo Sapien 902His Ile Ser Tyr Pro Pro Leu His Glu Arg Ala 1 5 10 903 9 PRT Homo Sapien903 Gln Thr Ala Ser Ser Ser Ser Thr Leu 1 5 904 10 PRT Homo Sapien 904Gln Thr Ala Ser Ser Ser Ser Thr Leu Val 1 5 10 905 9 PRT Homo Sapien 905Val Thr Leu Gly Glu Val Pro Ala Ala 1 5 906 10 PRT Homo Sapien 906 ValThr Lys Ala Glu Met Leu Glu Ser Val 1 5 10 907 11 PRT Homo Sapien 907Val Thr Lys Ala Glu Met Leu Glu Ser Val Leu 1 5 10 908 11 PRT HomoSapien 908 Val Thr Cys Leu Gly Leu Ser Tyr Asp Gly Leu 1 5 10 909 9 PRTHomo Sapien 909 Lys Thr Gly Leu Leu Ile Ile Val Leu 1 5 910 10 PRT HomoSapien 910 Lys Thr Gly Leu Leu Ile Ile Val Leu Ala 1 5 10 911 11 PRTHomo Sapien 911 Lys Thr Gly Leu Leu Ile Ile Val Leu Ala Ile 1 5 10 91211 PRT Homo Sapien 912 His Thr Leu Lys Ile Gly Gly Glu Pro His Ile 1 510 913 9 PRT Homo Sapien 913 Met Leu Asp Leu Gln Pro Glu Thr Thr 1 5 9149 PRT Homo Sapien 914 Gly Leu Glu Ala Arg Gly Glu Ala Leu 1 5 915 9 PRTHomo Sapien 915 Ala Leu Ser Arg Lys Val Ala Glu Leu 1 5 916 9 PRT HomoSapien 916 Phe Leu Trp Gly Pro Arg Ala Leu Val 1 5 917 10 PRT HomoSapien 917 Thr Leu Val Glu Val Thr Leu Gly Glu Val 1 5 10 918 10 PRTHomo Sapien 918 Ala Leu Ser Arg Lys Val Ala Glu Leu Val 1 5 10 919 10PRT Homo Sapien 919 Ala Leu Val Glu Thr Ser Tyr Val Lys Val 1 5 10 920 9PRT Homo Sapien 920 Tyr Met Asn Gly Thr Met Ser Gln Val 1 5 921 10 PRTHomo Sapien 921 Met Leu Leu Ala Val Leu Tyr Cys Leu Leu 1 5 10 922 9 PRTHomo Sapien 922 Met Leu Leu Ala Val Leu Tyr Cys Leu 1 5 923 9 PRT HomoSapien 923 Leu Leu Ala Val Leu Tyr Cys Leu Leu 1 5 924 13 PRT HomoSapien 924 Ser Glu Ile Trp Arg Asp Ile Asp Phe Ala His Glu Ala 1 5 10925 9 PRT Homo Sapien 925 Ser Glu Ile Trp Arg Asp Ile Asp Phe 1 5 926 10PRT Homo Sapien 926 Glu Glu Asn Leu Leu Asp Phe Val Arg Phe 1 5 10 92710 PRT Homo Sapien 927 Glu Ala Ala Gly Ile Gly Ile Leu Thr Val 1 5 10928 9 PRT Homo Sapien 928 Met Leu Leu Ala Val Leu Tyr Cys Leu 1 5 929 9PRT Homo Sapien 929 Tyr Met Asp Gly Thr Met Ser Gln Val 1 5 930 9 PRTHomo Sapien 930 Tyr Leu Glu Pro Gly Pro Val Thr Ala 1 5 931 10 PRT HomoSapien 931 Leu Leu Asp Gly Thr Ala Thr Leu Arg Leu 1 5 10 932 9 PRT HomoSapien 932 Gly Ile Leu Gly Phe Val Phe Thr Leu 1 5 933 9 PRT Homo Sapien933 Glu Ala Asp Pro Thr Gly His Ser Tyr 1 5 934 9 PRT Homo Sapien 934Glu Ala Asp Pro Thr Gly His Ser Tyr 1 5 935 22 PRT Homo Sapien 935 MetAla Ala Arg Ala Val Phe Leu Ala Leu Ser Ala Gln Leu Leu Gln 1 5 10 15Ala Arg Leu Met Lys Glu 20 936 16 PRT Homo Sapien 936 Met Ala Ala ArgAla Val Phe Leu Ala Leu Ser Ala Gln Leu Leu Gln 1 5 10 15 937 9 PRT HomoSapien 937 Ala Ala Arg Ala Val Phe Leu Ala Leu 1 5 938 9 PRT Influenza938 Ile Tyr Gln Arg Ile Arg Ala Leu Val 1 5 939 9 PRT Homo Sapien 939Ser Tyr Phe Pro Glu Ile Thr His Ile 1 5 940 9 PRT Influenza 940 Ile TyrAla Thr Val Ala Gly Ser Leu 1 5 941 9 PRT Influenza 941 Val Tyr Gln IleLeu Ala Ile Tyr Ala 1 5 942 9 PRT Influenza 942 Ile Tyr Ser Thr Val AlaSer Ser Leu 1 5 943 9 PRT Influenza 943 Leu Tyr Gln Asn Val Gly Thr TyrVal 1 5 944 9 PRT Homo Sapien 944 Arg Tyr Leu Glu Asn Gln Lys Arg Thr 15 945 9 PRT Homo Sapien 945 Arg Tyr Leu Lys Asn Gly Lys Glu Thr 1 5 9469 PRT Homo Sapien 946 Lys Tyr Gln Ala Val Thr Thr Thr Leu 1 5 947 9 PRTPlasmodium Berghei 947 Ser Tyr Ile Pro Ser Ala Glu Lys Ile 1 5 948 9 PRTPlasmodium Yoelii 948 Ser Tyr Val Pro Ser Ala Phe Gln Ile 1 5 949 8 PRTVesicular Stomatitis Virus 949 Arg Gly Tyr Val Tyr Gln Gly Leu 1 5 950 8PRT Gallus Domesticus 950 Ser Ile Ile Asn Phe Glu Lys Leu 1 5 951 8 PRTSendai Virus 951 Ala Pro Gly Asn Tyr Pro Ala Leu 1 5 952 9 PRT HomoSapien 952 Val Pro Tyr Gly Ser Phe Lys His Val 1 5 953 9 PRT Influenza953 Thr Tyr Gln Arg Thr Arg Ala Leu Val 1 5 954 9 PRT Homo Sapien 954Ser Tyr Phe Pro Glu Ile Thr His Ile 1 5 955 9 PRT Influenza 955 Ile TyrAla Thr Val Ala Gly Ser Leu 1 5 956 9 PRT Influenza 956 Val Tyr Gln IleLeu Ala Ile Tyr Ala 1 5 957 9 PRT Influenza 957 Ile Tyr Ser Thr Val AlaSer Ser Leu 1 5 958 9 PRT Influenza 958 Leu Tyr Gln Asn Val Gly Thr TyrVal 1 5 959 10 PRT Homo Sapien 959 Arg Tyr Leu Glu Asn Gly Lys Glu ThrLeu 1 5 10 960 10 PRT Homo Sapien 960 Arg Tyr Leu Lys Asn Gly Lys GluThr Leu 1 5 10 961 9 PRT Homo Sapien 961 Lys Tyr Gln Ala Val Thr Thr ThrLeu 1 5 962 9 PRT Plasmodium Berghei 962 Ser Tyr Ile Pro Ser Ala Glu LysIle 1 5 963 9 PRT Plasmodium Yoelii 963 Ser Tyr Val Pro Ser Ala Glu GlnIle 1 5 964 9 PRT Influenza 964 Ala Ser Asn Glu Asn Met Glu Thr Met 1 5965 10 PRT Adenovirus 965 Ser Gly Pro Ser Asn Thr Pro Pro Glu Ile 1 5 10966 11 PRT Lymphocytic Choriomeningitis Virus 966 Ser Gly Val Glu AsnPro Gly Gly Tyr Cys Leu 1 5 10 967 9 PRT Simian Virus VARIANT 7, 8, 9Xaa = Any Amino Acid 967 Ser Ala Ile Asn Asn Tyr Xaa Xaa Xaa 1 5 968 9PRT Human Immunodeficiency Virus 968 Ile Leu Lys Glu Pro Val His Gly Val1 5 969 9 PRT Influenza 969 Gly Ile Leu Gly Phe Val Phe Thr Leu 1 5 97010 PRT Influenza 970 Ile Leu Gly Phe Val Phe Thr Leu Thr Val 1 5 10 9719 PRT Human Immunodeficiency Virus 971 Phe Leu Gln Ser Arg Pro Glu ProThr 1 5 972 9 PRT Human Immunodeficiency Virus VARIANT 8, 9 Xaa = AnyAmino Acid 972 Ala Met Gln Met Leu Lys Glu Xaa Xaa 1 5 973 9 PRT HumanImmunodeficiency Virus 973 Pro Ile Ala Pro Gly Gln Met Arg Glu 1 5 974 9PRT Human Immunodeficiency Virus 974 Gln Met Lys Asp Cys Thr Glu Arg Gln1 5 975 7 PRT Human Immunodeficiency Virus 975 Val Tyr Gly Val Ile GlnLys 1 5 976 12 PRT Artificial Sequence Synthetic HLA-A2 binding nonamerpeptide 976 Ser Asp Leu Arg Gly Tyr Val Tyr Gln Gly Leu Lys 1 5 10 97715 PRT Artificial Sequence Epitope mimic of natural tumor Ag 977 Arg ProGln Ala Ser Gly Val Tyr Met Gly Asn Leu Thr Thr Gln 1 5 10 15 978 9 PRTArtificial Sequence Epitope mimic of natural tumor Ag 978 Lys Ala ValTyr Asn Phe Ala Thr Cys 1 5 979 9 PRT Homo Sapien 979 Glu Val Asp ProAla Ser Asn Thr Tyr 1 5

What is claimed is:
 1. An isolated nucleic acid comprising a readingframe comprising a first sequence, wherein said first sequence encodesone or more segments of tumor-associated antigen SSX-2 (SEQ ID NO: 40),wherein the first sequence does not encode the complete SSX-2 antigen,and wherein each segment comprises an epitope cluster, said clustercomprising or encoding at least two amino acid sequences having a knownor predicted affinity for a same MHC receptor peptide binding cleft. 2.The nucleic acid of claim 1, wherein said epitope cluster is chosen fromthe group consisting of amino acids 5-28, 16-28, 41-65, 57-67, 99-114,167-180, and 167-183 of SSX-2.
 3. The nucleic acid of claim 1, whereinsaid one or more segments consist of said epitope cluster.
 4. Thenucleic acid of claim 1, wherein said first sequence encodes a fragmentof SSX-2.
 5. The nucleic acid of claim 4, wherein said encoded fragmentconsists of a polypeptide having a length, wherein the length of thepolypeptide is less than about 90% of the length of SSX-2.
 6. Thenucleic acid of claim 4, wherein said encoded fragment consists of apolypeptide having a length, wherein the length of the polypeptide isless than about 80% of the length of SSX-2.
 7. The nucleic acid of claim4, wherein said encoded fragment consists of a polypeptide having alength, wherein the length of the polypeptide is less than about 60% ofthe length of SSX-2.
 8. The nucleic acid of claim 4, wherein saidencoded fragment consists of a polypeptide having a length, wherein thelength of the polypeptide is less than about 50% of the length of SSX-2.9. The nucleic acid of claim 4, wherein said encoded fragment consistsof a polypeptide having a length, wherein the length of the polypeptideis less than about 25% of the length of SSX-2.
 10. The nucleic acid ofclaim 4, wherein said encoded fragment consists of a polypeptide havinga length, wherein the length of the polypeptide is less than about 10%of the length of SSX-2.
 11. The nucleic acid of claim 4, wherein saidencoded fragment consists essentially of amino acids 5-65, 5-67, or5-114.
 12. The nucleic acid of claim 4, wherein said encoded fragmentconsists essentially of amino acids 16-65, 16-67, 16-114, 16-180, or16-183.
 13. The nucleic acid of claim 4, wherein said encoded fragmentconsists essentially of amino acids 41-67, 41-114, 41-180, or 41-183.14. The nucleic acid of claim 4, wherein said encoded fragment consistsessentially of amino acids 57-114, 57-180, or 57-183.
 15. The nucleicacid of claim 4, wherein said encoded fragment consists essentiallyamino acids 99-180 or 99-183.
 16. The nucleic acid of claim 4, whereinsaid encoded fragment consists essentially of amino acids 16-183 ofSSX-2.
 17. The nucleic acid of claim 16, wherein said first sequenceencodes exactly amino acids 15-183 of SSX-2.
 18. The nucleic acid ofclaim 4, wherein said encoded fragment consists essentially of an aminoacid sequence beginning at one of amino acids selected from the groupconsisting of 5, 16, 41, 57, and 99 of SSX-2, and ending at one of theamino acids selected from the group consisting of amino acid 65, 67,114, 180, and 183 of SSX-2
 19. The nucleic acid of claim 1, furthercomprising a second sequence, wherein the second sequence encodesessentially a housekeeping epitope.
 20. The nucleic acid of claim 1,wherein said reading frame is operably linked to a promoter.
 21. Thenucleic acid of claim 19, wherein said first and second sequencesconstitute a single reading frame.
 22. The nucleic acid of claim 21,wherein said reading frame is operably linked to a promoter.
 23. Anisolated polypeptide comprising the amino acid sequence encoded in saidreading frame of claim
 22. 24. An immunogenic composition comprising thenucleic acid of claim
 22. 25. An immunogenic composition comprising thepolypeptide of claim 23.